ID GOSR2_HUMAN Reviewed; 212 AA. AC O14653; D3DXJ5; D3DXJ6; Q8N4B8; Q96DA5; Q9BZZ4; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 30-AUG-2002, sequence version 2. DT 27-MAR-2024, entry version 195. DE RecName: Full=Golgi SNAP receptor complex member 2; DE AltName: Full=27 kDa Golgi SNARE protein; DE AltName: Full=Membrin; GN Name=GOSR2; Synonyms=GS27; 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] (ISOFORM A), FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=9349823; DOI=10.1038/39923; RA Lowe S.L., Peter F., Subramaniam V.N., Wong S.H., Hong W.; RT "A SNARE involved in protein transport through the Golgi apparatus."; RL Nature 389:881-884(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A). RX PubMed=10198168; DOI=10.1006/geno.1998.5649; RA Bui T.D., Levy E.R., Subramaniam V.N., Lowe S.L., Hong W.; RT "cDNA characterization and chromosomal mapping of human Golgi SNARE GS27 RT and GS28 to chromosome 17."; RL Genomics 57:285-288(1999). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B). RA Bui T.D., Hong W.; RT "Gene organization of human Golgi SNARE GS27."; RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). 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=16625196; DOI=10.1038/nature04689; RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.; RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the RT human lineage."; RL Nature 440:1045-1049(2006). RN [6] 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND 3). RC TISSUE=Colon, and Lung; 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 [8] RP PROTEIN SEQUENCE OF 1-10; 51-63 AND 75-85, ACETYLATION AT MET-1, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Osteosarcoma; RA Bienvenut W.V., Lao L., Ryan K.M.; RL Submitted (JUN-2009) to UniProtKB. RN [9] {ECO:0007744|PDB:3EG9} RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 116-121 IN COMPLEX WITH SEC23A RP AND SEC24D, INTERACTION WITH SEC24C AND SEC24D, MUTAGENESIS OF ILE-118 AND RP MET-120, AND MOTIF. RX PubMed=18843296; DOI=10.1038/emboj.2008.208; RA Mancias J.D., Goldberg J.; RT "Structural basis of cargo membrane protein discrimination by the human RT COPII coat machinery."; RL EMBO J. 27:2918-2928(2008). RN [10] RP VARIANT EPM6 TRP-144, CHARACTERIZATION OF VARIANT EPM6 TRP-144, AND RP SUBCELLULAR LOCATION. RX PubMed=21549339; DOI=10.1016/j.ajhg.2011.04.011; RA Corbett M.A., Schwake M., Bahlo M., Dibbens L.M., Lin M., Gandolfo L.C., RA Vears D.F., O'Sullivan J.D., Robertson T., Bayly M.A., Gardner A.E., RA Vlaar A.M., Korenke G.C., Bloem B.R., de Coo I.F., Verhagen J.M., RA Lehesjoki A.E., Gecz J., Berkovic S.F.; RT "A mutation in the Golgi Qb-SNARE gene GOSR2 causes progressive myoclonus RT epilepsy with early ataxia."; RL Am. J. Hum. Genet. 88:657-663(2011). RN [11] RP VARIANT EPM6 TRP-144. RX PubMed=24458321; DOI=10.1002/mds.25704; RA van Egmond M.E., Verschuuren-Bemelmans C.C., Nibbeling E.A., Elting J.W., RA Sival D.A., Brouwer O.F., de Vries J.J., Kremer H.P., Sinke R.J., RA Tijssen M.A., de Koning T.J.; RT "Ramsay Hunt syndrome: clinical characterization of progressive myoclonus RT ataxia caused by GOSR2 mutation."; RL Mov. Disord. 29:139-143(2014). RN [12] RP VARIANT MYOS TRP-144, AND INVOLVEMENT IN MYOS. RX PubMed=29855340; DOI=10.1186/s13395-018-0163-0; RA Larson A.A., Baker P.R. II, Milev M.P., Press C.A., Sokol R.J., Cox M.O., RA Lekostaj J.K., Stence A.A., Bossler A.D., Mueller J.M., Prematilake K., RA Tadjo T.F., Williams C.A., Sacher M., Moore S.A.; RT "TRAPPC11 and GOSR2 mutations associate with hypoglycosylation of alpha- RT dystroglycan and muscular dystrophy."; RL Skelet. Muscle 8:17-17(2018). RN [13] RP VARIANTS MYOS 28-GLN--THR-212 DEL AND TRP-144. RX PubMed=33639315; DOI=10.1016/j.ejmg.2021.104184; RA Henige H., Kaur S., Pappas K.; RT "Compound heterozygous variants in GOSR2 associated with congenital RT muscular dystrophy: A case report."; RL Eur. J. Med. Genet. 64:104184-104184(2021). RN [14] RP VARIANT MYOS 107-ARG--THR-212 DEL. RX PubMed=34167170; DOI=10.1002/humu.24247; RA Stemmerik M.G., Borch J.S., Dunoe M., Krag T., Vissing J.; RT "Myopathy can be a key phenotype of membrin (GOSR2) deficiency."; RL Hum. Mutat. 42:1101-1106(2021). CC -!- FUNCTION: Involved in transport of proteins from the cis/medial-Golgi CC to the trans-Golgi network. {ECO:0000269|PubMed:9349823}. CC -!- SUBUNIT: Part of a unique SNARE complex composed of the Golgi SNAREs CC GOSR1, STX5 and YKT6 (By similarity). Interacts (via IxM motif) with CC SEC24C and SEC24D; mediates GOSR2 packaging into COPII-coated vesicles CC (PubMed:18843296). {ECO:0000250|UniProtKB:O35165, CC ECO:0000269|PubMed:18843296}. CC -!- INTERACTION: CC O14653; Q13520: AQP6; NbExp=3; IntAct=EBI-4401517, EBI-13059134; CC O14653; Q3SXY8: ARL13B; NbExp=3; IntAct=EBI-4401517, EBI-11343438; CC O14653; O15155: BET1; NbExp=5; IntAct=EBI-4401517, EBI-749204; CC O14653; P62952: BLCAP; NbExp=3; IntAct=EBI-4401517, EBI-3895726; CC O14653; Q96BA8: CREB3L1; NbExp=5; IntAct=EBI-4401517, EBI-6942903; CC O14653; P49447: CYB561; NbExp=3; IntAct=EBI-4401517, EBI-8646596; CC O14653; Q53TN4: CYBRD1; NbExp=3; IntAct=EBI-4401517, EBI-8637742; CC O14653; Q15125: EBP; NbExp=3; IntAct=EBI-4401517, EBI-3915253; CC O14653; Q9GZR5: ELOVL4; NbExp=3; IntAct=EBI-4401517, EBI-18535450; CC O14653; Q9NYP7: ELOVL5; NbExp=3; IntAct=EBI-4401517, EBI-11037623; CC O14653; Q8TBP5: FAM174A; NbExp=3; IntAct=EBI-4401517, EBI-18636064; CC O14653; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-4401517, EBI-18304435; CC O14653; Q969F0: FATE1; NbExp=3; IntAct=EBI-4401517, EBI-743099; CC O14653; Q0D2H9: GOLGA8DP; NbExp=5; IntAct=EBI-4401517, EBI-10181276; CC O14653; Q08AF8: GOLGA8G; NbExp=5; IntAct=EBI-4401517, EBI-10181260; CC O14653; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-4401517, EBI-13345167; CC O14653; O15529: GPR42; NbExp=3; IntAct=EBI-4401517, EBI-18076404; CC O14653; Q8TED1: GPX8; NbExp=3; IntAct=EBI-4401517, EBI-11721746; CC O14653; P31937: HIBADH; NbExp=3; IntAct=EBI-4401517, EBI-11427100; CC O14653; Q7Z5P4: HSD17B13; NbExp=3; IntAct=EBI-4401517, EBI-18053395; CC O14653; Q9Y5U9: IER3IP1; NbExp=3; IntAct=EBI-4401517, EBI-725665; CC O14653; Q8N5M9: JAGN1; NbExp=3; IntAct=EBI-4401517, EBI-10266796; CC O14653; Q8N6L0: KASH5; NbExp=6; IntAct=EBI-4401517, EBI-749265; CC O14653; A8MZ59: LEUTX; NbExp=3; IntAct=EBI-4401517, EBI-17490413; CC O14653; Q9H400: LIME1; NbExp=3; IntAct=EBI-4401517, EBI-2830566; CC O14653; Q5T0T0: MARCHF8; NbExp=3; IntAct=EBI-4401517, EBI-14061946; CC O14653; Q9GZY8-5: MFF; NbExp=3; IntAct=EBI-4401517, EBI-11956541; CC O14653; Q5SR56: MFSD14B; NbExp=3; IntAct=EBI-4401517, EBI-373355; CC O14653; Q6N075: MFSD5; NbExp=3; IntAct=EBI-4401517, EBI-3920969; CC O14653; Q8N4V1: MMGT1; NbExp=3; IntAct=EBI-4401517, EBI-6163737; CC O14653; Q96FA3: PELI1; NbExp=3; IntAct=EBI-4401517, EBI-448369; CC O14653; Q86VR2: RETREG3; NbExp=3; IntAct=EBI-4401517, EBI-10192441; CC O14653; Q7Z5B4-5: RIC3; NbExp=3; IntAct=EBI-4401517, EBI-12375429; CC O14653; Q6ZMZ0: RNF19B; NbExp=3; IntAct=EBI-4401517, EBI-2466594; CC O14653; Q14973: SLC10A1; NbExp=3; IntAct=EBI-4401517, EBI-3923031; CC O14653; Q3KNW5: SLC10A6; NbExp=3; IntAct=EBI-4401517, EBI-18159983; CC O14653; Q9NPE6: SPAG4; NbExp=3; IntAct=EBI-4401517, EBI-10819434; CC O14653; Q16623: STX1A; NbExp=6; IntAct=EBI-4401517, EBI-712466; CC O14653; Q12846: STX4; NbExp=6; IntAct=EBI-4401517, EBI-744942; CC O14653; Q13190: STX5; NbExp=3; IntAct=EBI-4401517, EBI-714206; CC O14653; O43752: STX6; NbExp=3; IntAct=EBI-4401517, EBI-2695795; CC O14653; Q96MV1: TLCD4; NbExp=3; IntAct=EBI-4401517, EBI-12947623; CC O14653; Q96DZ7: TM4SF19; NbExp=3; IntAct=EBI-4401517, EBI-6448756; CC O14653; Q8N6Q1: TMCO5A; NbExp=3; IntAct=EBI-4401517, EBI-12821895; CC O14653; Q96A25: TMEM106A; NbExp=3; IntAct=EBI-4401517, EBI-3915978; CC O14653; Q9BVX2: TMEM106C; NbExp=3; IntAct=EBI-4401517, EBI-2821497; CC O14653; Q6UW68: TMEM205; NbExp=3; IntAct=EBI-4401517, EBI-6269551; CC O14653; Q53FP2: TMEM35A; NbExp=3; IntAct=EBI-4401517, EBI-11722971; CC -!- SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane CC {ECO:0000269|PubMed:21549339}; Single-pass type IV membrane protein CC {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:9349823}. CC Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O35165}. CC Note=Concentrated most in the intermediate compartment/cis-Golgi CC network and the cis-Golgi cisternae 1 and 2. Greatly reduced in CC concentration at the trans end of the Golgi apparatus. CC {ECO:0000250|UniProtKB:O35165}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=A; CC IsoId=O14653-1; Sequence=Displayed; CC Name=B; CC IsoId=O14653-2; Sequence=VSP_001829; CC Name=3; CC IsoId=O14653-3; Sequence=VSP_043200; CC -!- DISEASE: Epilepsy, progressive myoclonic 6 (EPM6) [MIM:614018]: A form CC of progressive myoclonic epilepsy, a clinically and genetically CC heterogeneous group of disorders defined by the combination of action CC and reflex myoclonus, other types of epileptic seizures, and CC progressive neurodegeneration and neurocognitive impairment. EPM6 is an CC autosomal recessive form characterized by onset of ataxia in the first CC years of life, followed by action myoclonus and seizures later in CC childhood, and loss of independent ambulation in the second decade. CC Cognition is not usually affected, although mild memory difficulties CC may occur in the third decade. {ECO:0000269|PubMed:21549339, CC ECO:0000269|PubMed:24458321}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Muscular dystrophy, congenital, with or without seizures CC (MYOS) [MIM:620166]: An autosomal recessive muscular dystrophy CC characterized by hypotonia and elevated serum creatine kinase levels CC apparent from birth. Patients have progressive muscle weakness, CC areflexia, and may develop seizures in early childhood or have abnormal CC epileptiform findings on electroencephalogram studies. CC {ECO:0000269|PubMed:29855340, ECO:0000269|PubMed:33639315, CC ECO:0000269|PubMed:34167170}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the GOSR2 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; AF007548; AAB82651.1; -; mRNA. DR EMBL; AF229796; AAK01855.1; -; mRNA. DR EMBL; AK290890; BAF83579.1; -; mRNA. DR EMBL; AC005670; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471231; EAW57694.1; -; Genomic_DNA. DR EMBL; CH471231; EAW57695.1; -; Genomic_DNA. DR EMBL; CH471231; EAW57699.1; -; Genomic_DNA. DR EMBL; CH471231; EAW57700.1; -; Genomic_DNA. DR EMBL; BC034762; AAH34762.1; -; mRNA. DR EMBL; BC009710; AAH09710.1; -; mRNA. DR CCDS; CCDS11507.1; -. [O14653-2] DR CCDS; CCDS42355.1; -. [O14653-1] DR CCDS; CCDS45719.1; -. [O14653-3] DR RefSeq; NP_001012529.1; NM_001012511.2. [O14653-3] DR RefSeq; NP_004278.2; NM_004287.4. [O14653-1] DR RefSeq; NP_473363.1; NM_054022.3. [O14653-2] DR PDB; 3EG9; X-ray; 3.00 A; C=116-121. DR PDBsum; 3EG9; -. DR AlphaFoldDB; O14653; -. DR SMR; O14653; -. DR BioGRID; 114940; 136. DR IntAct; O14653; 73. DR MINT; O14653; -. DR STRING; 9606.ENSP00000461784; -. DR iPTMnet; O14653; -. DR PhosphoSitePlus; O14653; -. DR SwissPalm; O14653; -. DR BioMuta; GOSR2; -. DR EPD; O14653; -. DR jPOST; O14653; -. DR MassIVE; O14653; -. DR MaxQB; O14653; -. DR PaxDb; 9606-ENSP00000225567; -. DR PeptideAtlas; O14653; -. DR ProteomicsDB; 48148; -. [O14653-1] DR ProteomicsDB; 48149; -. [O14653-2] DR ProteomicsDB; 48150; -. [O14653-3] DR Pumba; O14653; -. DR Antibodypedia; 3382; 169 antibodies from 25 providers. DR DNASU; 9570; -. DR Ensembl; ENST00000225567.9; ENSP00000225567.4; ENSG00000108433.17. [O14653-2] DR Ensembl; ENST00000640051.2; ENSP00000492751.1; ENSG00000108433.17. [O14653-1] DR Ensembl; ENST00000640621.1; ENSP00000492830.1; ENSG00000108433.17. [O14653-3] DR GeneID; 9570; -. DR KEGG; hsa:9570; -. DR MANE-Select; ENST00000640051.2; ENSP00000492751.1; NM_004287.5; NP_004278.2. DR UCSC; uc002iky.4; human. [O14653-1] DR AGR; HGNC:4431; -. DR CTD; 9570; -. DR DisGeNET; 9570; -. DR GeneCards; GOSR2; -. DR HGNC; HGNC:4431; GOSR2. DR HPA; ENSG00000108433; Low tissue specificity. DR MalaCards; GOSR2; -. DR MIM; 604027; gene. DR MIM; 614018; phenotype. DR MIM; 620166; phenotype. DR neXtProt; NX_O14653; -. DR OpenTargets; ENSG00000108433; -. DR Orphanet; 280620; Progressive myoclonic epilepsy type 6. DR PharmGKB; PA28816; -. DR VEuPathDB; HostDB:ENSG00000108433; -. DR eggNOG; KOG3251; Eukaryota. DR GeneTree; ENSGT00950000183192; -. DR InParanoid; O14653; -. DR OMA; RMRVDQL; -. DR OrthoDB; 5477092at2759; -. DR PhylomeDB; O14653; -. DR TreeFam; TF313702; -. DR PathwayCommons; O14653; -. DR Reactome; R-HSA-204005; COPII-mediated vesicle transport. DR Reactome; R-HSA-381038; XBP1(S) activates chaperone genes. DR Reactome; R-HSA-5694530; Cargo concentration in the ER. DR Reactome; R-HSA-6807878; COPI-mediated anterograde transport. DR Reactome; R-HSA-6811438; Intra-Golgi traffic. DR SignaLink; O14653; -. DR BioGRID-ORCS; 9570; 709 hits in 1161 CRISPR screens. DR ChiTaRS; GOSR2; human. DR EvolutionaryTrace; O14653; -. DR GeneWiki; GOSR2; -. DR GenomeRNAi; 9570; -. DR Pharos; O14653; Tbio. DR PRO; PR:O14653; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; O14653; Protein. DR Bgee; ENSG00000108433; Expressed in buccal mucosa cell and 202 other cell types or tissues. DR ExpressionAtlas; O14653; baseline and differential. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central. DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; TAS:Reactome. DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; IBA:GO_Central. DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA. DR GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB. DR GO; GO:0031902; C:late endosome membrane; IBA:GO_Central. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0031201; C:SNARE complex; ISS:UniProtKB. DR GO; GO:0005484; F:SNAP receptor activity; IBA:GO_Central. DR GO; GO:0000149; F:SNARE binding; IBA:GO_Central. DR GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IDA:UniProtKB. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR GO; GO:0006906; P:vesicle fusion; IBA:GO_Central. DR CDD; cd15863; SNARE_GS27; 1. DR Gene3D; 1.20.58.400; t-snare proteins; 1. DR InterPro; IPR027027; GOSR2/Membrin/Bos1. DR InterPro; IPR010989; SNARE. DR InterPro; IPR038407; v-SNARE_N_sf. DR PANTHER; PTHR21230:SF1; GOLGI SNAP RECEPTOR COMPLEX MEMBER 2; 1. DR PANTHER; PTHR21230; VESICLE TRANSPORT V-SNARE PROTEIN VTI1-RELATED; 1. DR Pfam; PF12352; V-SNARE_C; 1. DR PIRSF; PIRSF028865; Membrin-2; 1. DR SUPFAM; SSF58038; SNARE fusion complex; 1. DR SUPFAM; SSF47661; t-snare proteins; 1. DR Genevisible; O14653; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Coiled coil; KW Congenital muscular dystrophy; Direct protein sequencing; Disease variant; KW Endoplasmic reticulum; Epilepsy; Golgi apparatus; Membrane; KW Neurodegeneration; Protein transport; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1..212 FT /note="Golgi SNAP receptor complex member 2" FT /id="PRO_0000212549" FT TOPO_DOM 1..190 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 191..211 FT /note="Helical; Anchor for type IV membrane protein" FT /evidence="ECO:0000255" FT TOPO_DOM 212 FT /note="Vesicular" FT /evidence="ECO:0000255" FT COILED 61..107 FT /evidence="ECO:0000255" FT MOTIF 118..120 FT /note="IxM motif; signal for cargo packaging into COPII- FT coated vesicles" FT /evidence="ECO:0000269|PubMed:18843296" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000269|Ref.8" FT VAR_SEQ 160..212 FT /note="GTQKKILDIANMLGLSNTVMRLIEKRAFQDKYFMIGGMLLTCVVMFLVVQYL FT T -> VGSLLGDREKASCFSLIQQFSNCVYILITCPQIVIF (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334" FT /id="VSP_043200" FT VAR_SEQ 196..212 FT /note="GMLLTCVVMFLVVQYLT -> TQGSCQTAHFGGRSAGSS (in isoform FT B)" FT /evidence="ECO:0000303|Ref.3" FT /id="VSP_001829" FT VARIANT 28..212 FT /note="Missing (in MYOS)" FT /evidence="ECO:0000269|PubMed:33639315" FT /id="VAR_087912" FT VARIANT 67 FT /note="R -> K (in dbSNP:rs197922)" FT /id="VAR_024471" FT VARIANT 107..212 FT /note="Missing (in MYOS)" FT /evidence="ECO:0000269|PubMed:34167170" FT /id="VAR_087913" FT VARIANT 144 FT /note="G -> W (in EPM6 and MYOS; no effect on protein FT stability; loss of localization to the cis-Golgi network FT membrane; loss of function; unable to rescue the yeast FT strain lacking the ortholog Bos1; dbSNP:rs387906881)" FT /evidence="ECO:0000269|PubMed:21549339, FT ECO:0000269|PubMed:24458321, ECO:0000269|PubMed:29855340, FT ECO:0000269|PubMed:33639315" FT /id="VAR_065833" FT MUTAGEN 118 FT /note="I->A: Loss of interaction with SEC24C." FT /evidence="ECO:0000269|PubMed:18843296" FT MUTAGEN 120 FT /note="M->A: Loss of interaction with SEC24C." FT /evidence="ECO:0000269|PubMed:18843296" FT CONFLICT 106 FT /note="S -> C (in Ref. 1; AAB82651)" FT /evidence="ECO:0000305" FT CONFLICT 113 FT /note="D -> G (in Ref. 1; AAB82651)" FT /evidence="ECO:0000305" FT CONFLICT 166 FT /note="L -> P (in Ref. 1; AAB82651)" FT /evidence="ECO:0000305" FT STRAND 117..119 FT /evidence="ECO:0007829|PDB:3EG9" SQ SEQUENCE 212 AA; 24775 MW; 4D5585CF858A610F CRC64; MDPLFQQTHK QVHEIQSCMG RLETADKQSV HIVENEIQAS IDQIFSRLER LEILSSKEPP NKRQNARLRV DQLKYDVQHL QTALRNFQHR RHAREQQERQ REELLSRTFT TNDSDTTIPM DESLQFNSSL QKVHNGMDDL ILDGHNILDG LRTQRLTLKG TQKKILDIAN MLGLSNTVMR LIEKRAFQDK YFMIGGMLLT CVVMFLVVQY LT //