TM230_HUMAN
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 03-AUG-2022, entry version 154.
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};
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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 CCDS; CCDS33438.1; -. [Q96A57-2]
DR RefSeq; NP_001009923.1; NM_001009923.1. [Q96A57-2]
DR RefSeq; NP_001009924.1; NM_001009924.1. [Q96A57-1]
DR RefSeq; NP_001009925.1; NM_001009925.1. [Q96A57-1]
DR RefSeq; NP_001317913.1; NM_001330984.1. [Q96A57-1]
DR RefSeq; NP_001317914.1; NM_001330985.1. [Q96A57-1]
DR RefSeq; NP_001317915.1; NM_001330986.1. [Q96A57-1]
DR RefSeq; NP_054864.3; NM_014145.4. [Q96A57-1]
DR RefSeq; XP_016883325.1; XM_017027836.1. [Q96A57-1]
DR AlphaFoldDB; Q96A57; -.
DR BioGRID; 118834; 48.
DR IntAct; Q96A57; 22.
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 EPD; Q96A57; -.
DR jPOST; Q96A57; -.
DR MassIVE; Q96A57; -.
DR MaxQB; Q96A57; -.
DR PaxDb; Q96A57; -.
DR PeptideAtlas; Q96A57; -.
DR PRIDE; Q96A57; -.
DR ProteomicsDB; 75916; -. [Q96A57-1]
DR ProteomicsDB; 75917; -. [Q96A57-2]
DR TopDownProteomics; Q96A57-1; -. [Q96A57-1]
DR TopDownProteomics; Q96A57-2; -. [Q96A57-2]
DR Antibodypedia; 2275; 186 antibodies from 23 providers.
DR DNASU; 29058; -.
DR Ensembl; ENST00000202834.11; ENSP00000202834.7; ENSG00000089063.15. [Q96A57-1]
DR Ensembl; ENST00000342308.10; ENSP00000341364.5; ENSG00000089063.15. [Q96A57-2]
DR Ensembl; ENST00000379277.6; ENSP00000368579.2; ENSG00000089063.15. [Q96A57-1]
DR Ensembl; ENST00000379279.6; ENSP00000368581.2; ENSG00000089063.15. [Q96A57-1]
DR Ensembl; ENST00000379283.6; ENSP00000368585.2; ENSG00000089063.15. [Q96A57-1]
DR Ensembl; ENST00000379286.6; ENSP00000368588.2; ENSG00000089063.15. [Q96A57-1]
DR Ensembl; ENST00000379299.6; ENSP00000368601.2; ENSG00000089063.15. [Q96A57-1]
DR GeneID; 29058; -.
DR KEGG; hsa:29058; -.
DR MANE-Select; ENST00000342308.10; ENSP00000341364.5; NM_001009923.2; NP_001009923.1. [Q96A57-2]
DR UCSC; uc002wlk.4; human. [Q96A57-1]
DR CTD; 29058; -.
DR DisGeNET; 29058; -.
DR GeneCards; TMEM230; -.
DR HGNC; HGNC:15876; TMEM230.
DR HPA; ENSG00000089063; Low tissue specificity.
DR MIM; 168600; phenotype.
DR MIM; 617019; gene.
DR neXtProt; NX_Q96A57; -.
DR OpenTargets; ENSG00000089063; -.
DR PharmGKB; PA25746; -.
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; 1357985at2759; -.
DR PhylomeDB; Q96A57; -.
DR TreeFam; TF329240; -.
DR PathwayCommons; Q96A57; -.
DR SignaLink; Q96A57; -.
DR BioGRID-ORCS; 29058; 74 hits in 1050 CRISPR screens.
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 102 other tissues.
DR ExpressionAtlas; Q96A57; baseline and differential.
DR Genevisible; Q96A57; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005776; C:autophagosome; IEA:UniProtKB-SubCell.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005770; C:late endosome; IDA:UniProtKB.
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:0048489; P:synaptic vesicle transport; IMP:UniProtKB.
DR InterPro; IPR044234; TMEM230.
DR InterPro; IPR008590; TMEM_230/134.
DR PANTHER; PTHR15664; PTHR15664; 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; Reference proteome; Synapse; Transmembrane;
KW 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; sporadic case; unknown pathological
FT significance; results in decreased synaptic vesicle
FT trafficking; dbSNP:rs1056737920)"
FT /evidence="ECO:0000269|PubMed:27270108"
FT /id="VAR_076713"
FT VARIANT 78
FT /note="R -> L (in PARK; unknown pathological significance;
FT results in decreased synaptic vesicle trafficking;
FT 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
