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 27-MAR-2024, entry version 185. 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}. 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; 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 PDB; 8A6M; NMR; -; A=1-195. DR PDBsum; 8A6M; -. DR AlphaFoldDB; O43759; -. DR SMR; O43759; -. DR BioGRID; 114592; 120. DR IntAct; O43759; 34. DR MINT; O43759; -. DR STRING; 9606.ENSP00000332287; -. DR GlyGen; O43759; 1 site, 1 O-linked glycan (1 site). 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; 9606-ENSP00000332287; -. DR PeptideAtlas; O43759; -. DR ProteomicsDB; 49150; -. [O43759-1] DR ProteomicsDB; 49151; -. [O43759-2] DR ProteomicsDB; 49152; -. [O43759-3] DR Pumba; O43759; -. DR TopDownProteomics; O43759-1; -. [O43759-1] DR Antibodypedia; 26612; 201 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 AGR; HGNC:11498; -. 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; WAFIWFV; -. DR OrthoDB; 4177492at2759; -. DR PhylomeDB; O43759; -. DR TreeFam; TF320995; -. DR PathwayCommons; O43759; -. DR Reactome; R-HSA-6798695; Neutrophil degranulation. DR SignaLink; O43759; -. DR BioGRID-ORCS; 9145; 17 hits in 1147 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 204 other cell types or tissues. DR ExpressionAtlas; O43759; baseline and differential. DR GO; GO:0035577; C:azurophil granule membrane; TAS:Reactome. DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; NAS:UniProtKB. 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; SYNAPTOGYRIN; 1. DR PANTHER; PTHR10838:SF7; SYNAPTOGYRIN-1; 1. DR Pfam; PF01284; MARVEL; 1. DR PIRSF; PIRSF011282; Synaptogyrin; 1. DR PROSITE; PS51225; MARVEL; 1. DR Genevisible; O43759; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Cytoplasmic vesicle; KW Membrane; 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" FT TURN 17..19 FT /evidence="ECO:0007829|PDB:8A6M" FT HELIX 20..22 FT /evidence="ECO:0007829|PDB:8A6M" FT HELIX 24..46 FT /evidence="ECO:0007829|PDB:8A6M" FT HELIX 48..53 FT /evidence="ECO:0007829|PDB:8A6M" FT TURN 57..59 FT /evidence="ECO:0007829|PDB:8A6M" FT HELIX 63..90 FT /evidence="ECO:0007829|PDB:8A6M" FT HELIX 98..133 FT /evidence="ECO:0007829|PDB:8A6M" FT HELIX 140..142 FT /evidence="ECO:0007829|PDB:8A6M" FT HELIX 145..173 FT /evidence="ECO:0007829|PDB:8A6M" 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 //