SNG1_HUMAN
ID SNG1_HUMAN Reviewed; 233 AA.
AC O43759; A6NP69; A8K0E2; O43757; O43758; Q53Y02; Q96J56; Q9UGZ4;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Synaptogyrin-1 {ECO:0000305};
GN Name=SYNGR1 {ECO:0000312|HGNC:HGNC:11498};
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 [MRNA] (ISOFORMS 1A; 1B AND 1C), AND VARIANT ASN-202
RP INS.
RX PubMed=9760194; DOI=10.1007/s004390050795;
RA Kedra D., Pan H.-Q., Seroussi E., Fransson I., Guilbaud C., Collins J.E.,
RA Dunham I., Blennow E., Roe B.A., Piehl F., Dumanski J.P.;
RT "Characterization of the human synaptogyrin gene family.";
RL Hum. Genet. 103:131-141(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1A), AND VARIANT ASN-202
RP INS.
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1B).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1A), AND VARIANT ASN-202
RP INS.
RC TISSUE=Cerebellum;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1B).
RC TISSUE=Brain;
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 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Melanoma;
RX PubMed=17081065; DOI=10.1021/pr060363j;
RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J.,
RA Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S.,
RA Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.;
RT "Proteomic and bioinformatic characterization of the biogenesis and
RT function of melanosomes.";
RL J. Proteome Res. 5:3135-3144(2006).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP VARIANTS ASN-202 INS AND GLY-222.
RX PubMed=17049558; DOI=10.1016/j.jpsychires.2006.08.010;
RA Cheng M.C., Chen C.H.;
RT "Identification of rare mutations of synaptogyrin 1 gene in patients with
RT schizophrenia.";
RL J. Psychiatr. Res. 41:1027-1031(2007).
CC -!- FUNCTION: May play a role in regulated exocytosis. Modulates the
CC localization of synaptophysin/SYP into synaptic-like microvesicles and
CC may therefore play a role in synaptic-like microvesicle formation
CC and/or maturation (By similarity). Involved in the regulation of short-
CC term and long-term synaptic plasticity (By similarity).
CC {ECO:0000250|UniProtKB:O55100, ECO:0000250|UniProtKB:Q62876}.
CC -!- INTERACTION:
CC O43759; Q969F0: FATE1; NbExp=3; IntAct=EBI-6269521, EBI-743099;
CC O43759-2; P29274: ADORA2A; NbExp=3; IntAct=EBI-12187159, EBI-2902702;
CC O43759-2; Q13520: AQP6; NbExp=3; IntAct=EBI-12187159, EBI-13059134;
CC O43759-2; O43889-2: CREB3; NbExp=3; IntAct=EBI-12187159, EBI-625022;
CC O43759-2; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-12187159, EBI-6942903;
CC O43759-2; Q15125: EBP; NbExp=3; IntAct=EBI-12187159, EBI-3915253;
CC O43759-2; Q08426: EHHADH; NbExp=3; IntAct=EBI-12187159, EBI-2339219;
CC O43759-2; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-12187159, EBI-781551;
CC O43759-2; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-12187159, EBI-18304435;
CC O43759-2; Q969F0: FATE1; NbExp=6; IntAct=EBI-12187159, EBI-743099;
CC O43759-2; O15529: GPR42; NbExp=3; IntAct=EBI-12187159, EBI-18076404;
CC O43759-2; O00219-2: HAS3; NbExp=3; IntAct=EBI-12187159, EBI-17186025;
CC O43759-2; O15243: LEPROT; NbExp=3; IntAct=EBI-12187159, EBI-15672507;
CC O43759-2; Q96E29: MTERF3; NbExp=3; IntAct=EBI-12187159, EBI-7825321;
CC O43759-2; Q9HB07: MYG1; NbExp=3; IntAct=EBI-12187159, EBI-709754;
CC O43759-2; Q9ULP0-2: NDRG4; NbExp=3; IntAct=EBI-12187159, EBI-11978907;
CC O43759-2; Q96CS7: PLEKHB2; NbExp=3; IntAct=EBI-12187159, EBI-373552;
CC O43759-2; O60664: PLIN3; NbExp=3; IntAct=EBI-12187159, EBI-725795;
CC O43759-2; Q96T60: PNKP; NbExp=3; IntAct=EBI-12187159, EBI-1045072;
CC O43759-2; Q86VR2: RETREG3; NbExp=3; IntAct=EBI-12187159, EBI-10192441;
CC O43759-2; O00560: SDCBP; NbExp=3; IntAct=EBI-12187159, EBI-727004;
CC O43759-2; Q3KNW5: SLC10A6; NbExp=3; IntAct=EBI-12187159, EBI-18159983;
CC O43759-2; Q13596: SNX1; NbExp=3; IntAct=EBI-12187159, EBI-2822329;
CC O43759-2; Q9NZD8: SPG21; NbExp=3; IntAct=EBI-12187159, EBI-742688;
CC O43759-2; Q6ZMD2-2: SPNS3; NbExp=3; IntAct=EBI-12187159, EBI-17848320;
CC O43759-2; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-12187159, EBI-8638294;
CC O43759-2; Q96B21: TMEM45B; NbExp=3; IntAct=EBI-12187159, EBI-3923061;
CC O43759-2; Q96HE8: TMEM80; NbExp=3; IntAct=EBI-12187159, EBI-11742770;
CC O43759-2; Q86WB7-2: UNC93A; NbExp=3; IntAct=EBI-12187159, EBI-13356252;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC vesicle membrane {ECO:0000250|UniProtKB:Q62876}; Multi-pass membrane
CC protein {ECO:0000250|UniProtKB:Q62876}. Melanosome
CC {ECO:0000269|PubMed:17081065}. Note=Identified by mass spectrometry in
CC melanosome fractions from stage I to stage IV.
CC {ECO:0000269|PubMed:17081065}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1A;
CC IsoId=O43759-1; Sequence=Displayed;
CC Name=1B;
CC IsoId=O43759-2; Sequence=VSP_006332;
CC Name=1C;
CC IsoId=O43759-3; Sequence=VSP_006331, VSP_006332;
CC -!- SIMILARITY: Belongs to the synaptogyrin family. {ECO:0000305}.
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DR EMBL; AJ002303; CAA05320.1; -; mRNA.
DR EMBL; AJ002304; CAA05321.1; -; mRNA.
DR EMBL; AJ002305; CAA05322.1; -; mRNA.
DR EMBL; CR456590; CAG30476.1; -; mRNA.
DR EMBL; BT007135; AAP35799.1; -; mRNA.
DR EMBL; AK289507; BAF82196.1; -; mRNA.
DR EMBL; AL022326; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000731; AAH00731.1; -; mRNA.
DR CCDS; CCDS13989.1; -. [O43759-1]
DR CCDS; CCDS13990.1; -. [O43759-2]
DR CCDS; CCDS13991.1; -. [O43759-3]
DR RefSeq; NP_004702.2; NM_004711.4. [O43759-1]
DR RefSeq; NP_663783.1; NM_145731.3. [O43759-2]
DR RefSeq; NP_663791.1; NM_145738.2. [O43759-3]
DR AlphaFoldDB; O43759; -.
DR BioGRID; 114592; 117.
DR IntAct; O43759; 33.
DR MINT; O43759; -.
DR STRING; 9606.ENSP00000332287; -.
DR iPTMnet; O43759; -.
DR PhosphoSitePlus; O43759; -.
DR SwissPalm; O43759; -.
DR BioMuta; SYNGR1; -.
DR EPD; O43759; -.
DR jPOST; O43759; -.
DR MassIVE; O43759; -.
DR MaxQB; O43759; -.
DR PaxDb; O43759; -.
DR PeptideAtlas; O43759; -.
DR PRIDE; O43759; -.
DR ProteomicsDB; 49150; -. [O43759-1]
DR ProteomicsDB; 49151; -. [O43759-2]
DR ProteomicsDB; 49152; -. [O43759-3]
DR TopDownProteomics; O43759-1; -. [O43759-1]
DR Antibodypedia; 26612; 184 antibodies from 31 providers.
DR DNASU; 9145; -.
DR Ensembl; ENST00000318801.8; ENSP00000318845.4; ENSG00000100321.15. [O43759-2]
DR Ensembl; ENST00000328933.10; ENSP00000332287.5; ENSG00000100321.15. [O43759-1]
DR Ensembl; ENST00000381535.4; ENSP00000370946.4; ENSG00000100321.15. [O43759-3]
DR GeneID; 9145; -.
DR KEGG; hsa:9145; -.
DR MANE-Select; ENST00000328933.10; ENSP00000332287.5; NM_004711.5; NP_004702.2.
DR UCSC; uc003axo.5; human. [O43759-1]
DR CTD; 9145; -.
DR DisGeNET; 9145; -.
DR GeneCards; SYNGR1; -.
DR HGNC; HGNC:11498; SYNGR1.
DR HPA; ENSG00000100321; Tissue enhanced (brain).
DR MIM; 603925; gene.
DR neXtProt; NX_O43759; -.
DR OpenTargets; ENSG00000100321; -.
DR PharmGKB; PA36280; -.
DR VEuPathDB; HostDB:ENSG00000100321; -.
DR eggNOG; KOG4016; Eukaryota.
DR GeneTree; ENSGT00950000182935; -.
DR HOGENOM; CLU_079186_0_1_1; -.
DR InParanoid; O43759; -.
DR OMA; NTCEWLT; -.
DR OrthoDB; 1549362at2759; -.
DR PhylomeDB; O43759; -.
DR TreeFam; TF320995; -.
DR PathwayCommons; O43759; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; O43759; -.
DR BioGRID-ORCS; 9145; 16 hits in 1069 CRISPR screens.
DR ChiTaRS; SYNGR1; human.
DR GeneWiki; SYNGR1; -.
DR GenomeRNAi; 9145; -.
DR Pharos; O43759; Tbio.
DR PRO; PR:O43759; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; O43759; protein.
DR Bgee; ENSG00000100321; Expressed in Brodmann (1909) area 10 and 202 other tissues.
DR ExpressionAtlas; O43759; baseline and differential.
DR Genevisible; O43759; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0035577; C:azurophil granule membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0030285; C:integral component of synaptic vesicle membrane; IEA:Ensembl.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0031594; C:neuromuscular junction; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0030672; C:synaptic vesicle membrane; IBA:GO_Central.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR GO; GO:0006605; P:protein targeting; IEA:Ensembl.
DR GO; GO:0045055; P:regulated exocytosis; ISS:UniProtKB.
DR GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; ISS:UniProtKB.
DR GO; GO:0048172; P:regulation of short-term neuronal synaptic plasticity; ISS:UniProtKB.
DR GO; GO:0048499; P:synaptic vesicle membrane organization; ISS:UniProtKB.
DR InterPro; IPR008253; Marvel.
DR InterPro; IPR016579; Synaptogyrin.
DR PANTHER; PTHR10838; PTHR10838; 1.
DR Pfam; PF01284; MARVEL; 1.
DR PIRSF; PIRSF011282; Synaptogyrin; 1.
DR PROSITE; PS51225; MARVEL; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasmic vesicle; Membrane;
KW Reference proteome; Synapse; Transmembrane; Transmembrane helix.
FT CHAIN 1..233
FT /note="Synaptogyrin-1"
FT /id="PRO_0000183990"
FT TOPO_DOM 1..23
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q62876"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 45..71
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q62876"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 93..103
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q62876"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 125..148
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q62876"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 170..233
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q62876"
FT DOMAIN 20..173
FT /note="MARVEL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00581"
FT REGION 194..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..233
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT VAR_SEQ 1..33
FT /note="MEGGAYGAGKAGGAFDPYTLVRQPHTILRVVSW -> MLTLEFGILEFDPSW
FT IGSWTQRSWVSWRSRPGCE (in isoform 1C)"
FT /evidence="ECO:0000303|PubMed:9760194"
FT /id="VSP_006331"
FT VAR_SEQ 162..233
FT /note="AGQAVLAFQRYQIGADSALFSQDYMDPSQDSSMPYAPYVEPTGPDPAGMGGT
FT YQQPANTFDTEPQGYQSQGY -> SLTAALAVRRFKDLSFQEEYSTLFPASAQP (in
FT isoform 1B and isoform 1C)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9760194, ECO:0000303|Ref.3"
FT /id="VSP_006332"
FT VARIANT 202
FT /note="P -> PN"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15461802, ECO:0000269|PubMed:17049558,
FT ECO:0000269|PubMed:9760194"
FT /id="VAR_060489"
FT VARIANT 222
FT /note="D -> G (in a patient affected by schizophrenia)"
FT /evidence="ECO:0000269|PubMed:17049558"
FT /id="VAR_060490"
SQ SEQUENCE 233 AA; 25456 MW; 8DE7000A46960213 CRC64;
MEGGAYGAGK AGGAFDPYTL VRQPHTILRV VSWLFSIVVF GSIVNEGYLN SASEGEEFCI
YNRNPNACSY GVAVGVLAFL TCLLYLALDV YFPQISSVKD RKKAVLSDIG VSAFWAFLWF
VGFCYLANQW QVSKPKDNPL NEGTDAARAA IAFSFFSIFT WAGQAVLAFQ RYQIGADSAL
FSQDYMDPSQ DSSMPYAPYV EPTGPDPAGM GGTYQQPANT FDTEPQGYQS QGY
