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GOSR2_HUMAN
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   03-AUG-2022, entry version 186.
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).
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}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry.
CC   -!- SIMILARITY: Belongs to the GOSR2 family. {ECO:0000305}.
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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; 122.
DR   IntAct; O14653; 70.
DR   MINT; O14653; -.
DR   STRING; 9606.ENSP00000225567; -.
DR   iPTMnet; O14653; -.
DR   PhosphoSitePlus; O14653; -.
DR   BioMuta; GOSR2; -.
DR   EPD; O14653; -.
DR   jPOST; O14653; -.
DR   MassIVE; O14653; -.
DR   MaxQB; O14653; -.
DR   PaxDb; O14653; -.
DR   PeptideAtlas; O14653; -.
DR   PRIDE; O14653; -.
DR   ProteomicsDB; 48148; -. [O14653-1]
DR   ProteomicsDB; 48149; -. [O14653-2]
DR   ProteomicsDB; 48150; -. [O14653-3]
DR   Antibodypedia; 3382; 154 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   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   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   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; 675 hits in 1083 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 200 other tissues.
DR   ExpressionAtlas; O14653; baseline and differential.
DR   Genevisible; O14653; HS.
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:UniProtKB.
DR   GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031902; C:late endosome membrane; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
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   Gene3D; 1.20.58.400; -; 1.
DR   InterPro; IPR027027; GOSR2/Membrin/Bos1.
DR   InterPro; IPR010989; SNARE.
DR   InterPro; IPR038407; v-SNARE_N_sf.
DR   PIRSF; PIRSF028865; Membrin-2; 1.
DR   SUPFAM; SSF47661; SSF47661; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Coiled coil;
KW   Direct protein sequencing; Disease variant; Endoplasmic reticulum;
KW   Epilepsy; Golgi apparatus; Membrane; Neurodegeneration; Protein transport;
KW   Reference proteome; Transmembrane; 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         67
FT                   /note="R -> K (in dbSNP:rs197922)"
FT                   /id="VAR_024471"
FT   VARIANT         144
FT                   /note="G -> W (in EPM6; no effect on protein stability;
FT                   loss of localization to the cis-Golgi network membrane;
FT                   loss of function; unable to rescue the yeast strain lacking
FT                   the ortholog Bos1; dbSNP:rs387906881)"
FT                   /evidence="ECO:0000269|PubMed:21549339"
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
 
 
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