ID TM230_HUMAN Reviewed; 120 AA. AC Q96A57; B2RDM8; D3DVZ9; Q0VGC8; Q5TDS5; Q96ES2; Q9P0A7; DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 28-JAN-2026, entry version 171. DE RecName: Full=Transmembrane protein 230; GN Name=TMEM230; Synonyms=C20orf30; ORFNames=HSPC274, UNQ2432/PRO4992; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Umbilical cord blood; RA Ye M., Zhang Q.-H., Zhou J., Shen Y., Wu X.-Y., Guan Z.Q., Wang L., RA Fan H.-Y., Mao Y.-F., Dai M., Huang Q.-H., Chen S.-J., Chen Z.; RT "Human partial CDS from CD34+ stem cells."; RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RX PubMed=12975309; DOI=10.1101/gr.1293003; RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A., RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.; RT "The secreted protein discovery initiative (SPDI), a large-scale effort to RT identify novel human secreted and transmembrane proteins: a bioinformatics RT assessment."; RL Genome Res. 13:2265-2270(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Skeletal muscle; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=11780052; DOI=10.1038/414865a; RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 20."; RL Nature 414:865-871(2001). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Bone marrow, Brain, Duodenum, Gall bladder, Lung, Ovary, and RC Prostate; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 AND SER-24, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [14] RP FUNCTION, SUBCELLULAR LOCATION, POSSIBLE INVOLVEMENT IN PARK, VARIANTS PARK RP CYS-29 AND LEU-78, VARIANT CYS-108, VARIANT THR-64 (ISOFORM 1), AND RP CHARACTERIZATION OF VARIANTS PARK CYS-29 AND LEU-78. RX PubMed=27270108; DOI=10.1038/ng.3589; RA Deng H.X., Shi Y., Yang Y., Ahmeti K.B., Miller N., Huang C., Cheng L., RA Zhai H., Deng S., Nuytemans K., Corbett N.J., Kim M.J., Deng H., Tang B., RA Yang Z., Xu Y., Chan P., Huang B., Gao X.P., Song Z., Liu Z., Fecto F., RA Siddique N., Foroud T., Jankovic J., Ghetti B., Nicholson D.A., Krainc D., RA Melen O., Vance J.M., Pericak-Vance M.A., Ma Y.C., Rajput A.H., RA Siddique T.; RT "Identification of TMEM230 mutations in familial Parkinson's disease."; RL Nat. Genet. 48:733-739(2016). CC -!- FUNCTION: Involved in trafficking and recycling of synaptic vesicles. CC {ECO:0000269|PubMed:27270108}. CC -!- INTERACTION: CC Q96A57-2; O43765: SGTA; NbExp=3; IntAct=EBI-17546822, EBI-347996; CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane CC protein {ECO:0000305}. Golgi apparatus, trans-Golgi network CC {ECO:0000269|PubMed:27270108}. Cytoplasmic vesicle, secretory vesicle, CC synaptic vesicle {ECO:0000269|PubMed:27270108}. Early endosome CC {ECO:0000269|PubMed:27270108}. Recycling endosome CC {ECO:0000269|PubMed:27270108}. Late endosome CC {ECO:0000269|PubMed:27270108}. Cytoplasmic vesicle, autophagosome CC {ECO:0000269|PubMed:27270108}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=2; CC IsoId=Q96A57-1; Sequence=Displayed; CC Name=1; CC IsoId=Q96A57-2; Sequence=VSP_018155; CC -!- DISEASE: Parkinson disease (PARK) [MIM:168600]: A complex CC neurodegenerative disorder characterized by bradykinesia, resting CC tremor, muscular rigidity and postural instability. Additional features CC are characteristic postural abnormalities, dysautonomia, dystonic CC cramps, and dementia. The pathology of Parkinson disease involves the CC loss of dopaminergic neurons in the substantia nigra and the presence CC of Lewy bodies (intraneuronal accumulations of aggregated proteins), in CC surviving neurons in various areas of the brain. The disease is CC progressive and usually manifests after the age of 50 years, although CC early-onset cases (before 50 years) are known. The majority of the CC cases are sporadic suggesting a multifactorial etiology based on CC environmental and genetic factors. However, some patients present with CC a positive family history for the disease. Familial forms of the CC disease usually begin at earlier ages and are associated with atypical CC clinical features. {ECO:0000269|PubMed:27270108}. Note=The gene CC represented in this entry may be involved in disease pathogenesis. CC Genetic variants in TMEM230 and DNAJC13 have been found in the same CC large multigenerational family with adult-onset Parkinson disease. The CC pathological role of each gene and therefore the exact molecular basis CC of the disease is unclear. {ECO:0000305|PubMed:27270108}. CC -!- SIMILARITY: Belongs to the TMEM134/TMEM230 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: [Isoform 1]: CC Sequence=AAF28952.1; Type=Frameshift; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF161392; AAF28952.1; ALT_FRAME; mRNA. DR EMBL; AY359115; AAQ89473.1; -; mRNA. DR EMBL; AK315606; BAG37975.1; -; mRNA. DR EMBL; AL121890; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL121924; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471133; EAX10431.1; -; Genomic_DNA. DR EMBL; CH471133; EAX10432.1; -; Genomic_DNA. DR EMBL; CH471133; EAX10433.1; -; Genomic_DNA. DR EMBL; CH471133; EAX10434.1; -; Genomic_DNA. DR EMBL; CH471133; EAX10437.1; -; Genomic_DNA. DR EMBL; BC070212; AAH70212.1; -; mRNA. DR EMBL; BC009768; AAH09768.1; -; mRNA. DR EMBL; BC009769; AAH09769.1; -; mRNA. DR EMBL; BC009770; AAH09770.1; -; mRNA. DR EMBL; BC011990; AAH11990.1; -; mRNA. DR EMBL; BC015113; AAH15113.1; -; mRNA. DR EMBL; BC110408; AAI10409.2; -; mRNA. DR CCDS; CCDS13086.1; -. [Q96A57-1] DR RefSeq; NP_001009924.1; NM_001009924.2. [Q96A57-1] DR RefSeq; NP_001009925.1; NM_001009925.2. [Q96A57-1] DR RefSeq; NP_001317913.1; NM_001330984.2. [Q96A57-1] DR RefSeq; NP_001317914.1; NM_001330985.2. [Q96A57-1] DR RefSeq; NP_001317915.1; NM_001330986.2. [Q96A57-1] DR RefSeq; NP_001410909.1; NM_001423980.1. [Q96A57-1] DR RefSeq; NP_054864.3; NM_014145.4. [Q96A57-1] DR AlphaFoldDB; Q96A57; -. DR BioGRID; 118834; 60. DR FunCoup; Q96A57; 1851. DR IntAct; Q96A57; 28. DR MINT; Q96A57; -. DR STRING; 9606.ENSP00000341364; -. DR TCDB; 9.B.232.1.1; the parkinson's disease tmem230 (tmem230) family. DR iPTMnet; Q96A57; -. DR PhosphoSitePlus; Q96A57; -. DR BioMuta; TMEM230; -. DR DMDM; 74751737; -. DR CPTAC; CPTAC-960; -. DR jPOST; Q96A57; -. DR MassIVE; Q96A57; -. DR PaxDb; 9606-ENSP00000341364; -. DR PeptideAtlas; Q96A57; -. DR ProteomicsDB; 75916; -. [Q96A57-1] DR ProteomicsDB; 75917; -. [Q96A57-2] DR Pumba; Q96A57; -. DR TopDownProteomics; Q96A57-1; -. [Q96A57-1] DR TopDownProteomics; Q96A57-2; -. [Q96A57-2] DR Antibodypedia; 2275; 190 antibodies from 23 providers. DR DNASU; 29058; -. DR Ensembl; ENST00000202834.12; ENSP00000202834.7; ENSG00000089063.17. [Q96A57-1] DR Ensembl; ENST00000342308.11; ENSP00000341364.6; ENSG00000089063.17. [Q96A57-1] DR Ensembl; ENST00000379277.7; ENSP00000368579.2; ENSG00000089063.17. [Q96A57-1] DR Ensembl; ENST00000379279.6; ENSP00000368581.2; ENSG00000089063.17. [Q96A57-1] DR Ensembl; ENST00000379283.6; ENSP00000368585.2; ENSG00000089063.17. [Q96A57-1] DR Ensembl; ENST00000379286.6; ENSP00000368588.2; ENSG00000089063.17. [Q96A57-1] DR Ensembl; ENST00000379299.6; ENSP00000368601.2; ENSG00000089063.17. [Q96A57-1] DR GeneID; 29058; -. DR KEGG; hsa:29058; -. DR MANE-Select; ENST00000202834.12; ENSP00000202834.7; NM_001009925.2; NP_001009925.1. DR UCSC; uc002wlk.4; human. [Q96A57-1] DR AGR; HGNC:15876; -. DR ClinPGx; PA25746; -. DR CTD; 29058; -. DR DisGeNET; 29058; -. DR GeneCards; TMEM230; -. DR HGNC; HGNC:15876; TMEM230. DR HPA; ENSG00000089063; Low tissue specificity. DR MalaCards; TMEM230; -. DR MIM; 168600; phenotype. DR MIM; 617019; gene. DR OpenTargets; ENSG00000089063; -. DR VEuPathDB; HostDB:ENSG00000089063; -. DR eggNOG; KOG4753; Eukaryota. DR GeneTree; ENSGT00390000008694; -. DR HOGENOM; CLU_126638_1_0_1; -. DR InParanoid; Q96A57; -. DR OMA; AYYAYYK; -. DR OrthoDB; 5597044at2759; -. DR PAN-GO; Q96A57; 3 GO annotations based on evolutionary models. DR PhylomeDB; Q96A57; -. DR PathwayCommons; Q96A57; -. DR SignaLink; Q96A57; -. DR Agora; ENSG00000089063; -. DR BioGRID-ORCS; 29058; 77 hits in 1128 CRISPR screens. DR CD-CODE; DEE660B4; Stress granule. DR ChiTaRS; TMEM230; human. DR GenomeRNAi; 29058; -. DR Pharos; Q96A57; Tbio. DR PRO; PR:Q96A57; -. DR Proteomes; UP000005640; Chromosome 20. DR RNAct; Q96A57; protein. DR Bgee; ENSG00000089063; Expressed in gall bladder and 104 other cell types or tissues. DR ExpressionAtlas; Q96A57; baseline and differential. DR GO; GO:0005776; C:autophagosome; IEA:UniProtKB-SubCell. DR GO; GO:0030424; C:axon; IEA:GOC. DR GO; GO:0005769; C:early endosome; IDA:UniProtKB. DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA. DR GO; GO:0005770; C:late endosome; IDA:UniProtKB. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. DR GO; GO:0055037; C:recycling endosome; IDA:UniProtKB. DR GO; GO:0008021; C:synaptic vesicle; IDA:UniProtKB. DR GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB. DR GO; GO:0098930; P:axonal transport; IDA:SynGO. DR GO; GO:0048489; P:synaptic vesicle transport; IMP:UniProtKB. DR InterPro; IPR044234; TMEM230. DR InterPro; IPR008590; TMEM_230/134. DR PANTHER; PTHR15664; C20ORF30 PROTEIN; 1. DR PANTHER; PTHR15664:SF6; TRANSMEMBRANE PROTEIN 230; 1. DR Pfam; PF05915; TMEM_230_134; 1. PE 1: Evidence at protein level; KW Alternative splicing; Cytoplasmic vesicle; Disease variant; Endosome; KW Golgi apparatus; Membrane; Neurodegeneration; Parkinson disease; KW Parkinsonism; Phosphoprotein; Proteomics identification; KW Reference proteome; Synapse; Transmembrane; Transmembrane helix. FT CHAIN 1..120 FT /note="Transmembrane protein 230" FT /id="PRO_0000233892" FT TRANSMEM 46..66 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 79..99 FT /note="Helical" FT /evidence="ECO:0000255" FT MOD_RES 15 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 23 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 24 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 1 FT /note="M -> MQPWALPTVGELWVCGRPGAALRWSLVLSPRLEPSGVISAHCNLHLL FT ASSDSSASASRLCQRVM (in isoform 1)" FT /evidence="ECO:0000303|Ref.1" FT /id="VSP_018155" FT VARIANT 29 FT /note="Y -> C (in PARK; uncertain significance; sporadic FT case; results in decreased synaptic vesicle trafficking; FT dbSNP:rs1056737920)" FT /evidence="ECO:0000269|PubMed:27270108" FT /id="VAR_076713" FT VARIANT 78 FT /note="R -> L (in PARK; uncertain significance; results in FT decreased synaptic vesicle trafficking; dbSNP:rs764786986)" FT /evidence="ECO:0000269|PubMed:27270108" FT /id="VAR_076714" FT VARIANT 108 FT /note="R -> C (in dbSNP:rs143571424)" FT /evidence="ECO:0000269|PubMed:27270108" FT /id="VAR_076715" FT CONFLICT 59..61 FT /note="LII -> SY (in Ref. 1; AAF28952)" FT /evidence="ECO:0000305" FT CONFLICT 109 FT /note="G -> A (in Ref. 6; AAH11990)" FT /evidence="ECO:0000305" FT VARIANT Q96A57-2:64 FT /note="M -> T (in dbSNP:rs141394228)" FT /evidence="ECO:0000269|PubMed:27270108" FT /id="VAR_082923" SQ SEQUENCE 120 AA; 13188 MW; 18A4A556330D77CE CRC64; MMPSRTNLAT GIPSSKVKYS RLSSTDDGYI DLQFKKTPPK IPYKAIALAT VLFLIGAFLI IIGSLLLSGY ISKGGADRAV PVLIIGILVF LPGFYHLRIA YYASKGYRGY SYDDIPDFDD //