STX5_HUMAN
ID STX5_HUMAN Reviewed; 355 AA.
AC Q13190; B2R8T2; F8W8Q9; Q5U0D4; Q7Z3T6; Q9BUG1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Syntaxin-5;
GN Name=STX5; Synonyms=STX5A;
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 2).
RC TISSUE=B-cell;
RX PubMed=9188044; DOI=10.1007/bf02736780;
RA Ravichandran V., Roche P.A.;
RT "Cloning and identification of human syntaxin 5 as a synaptobrevin/VAMP
RT binding protein.";
RL J. Mol. Neurosci. 8:159-161(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Heart;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Umbilical cord blood;
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 MRNA] (ISOFORM 2).
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 (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Kidney, and Uterus;
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 INTERACTION WITH COG4.
RX PubMed=19536132; DOI=10.1038/emboj.2009.168;
RA Laufman O., Kedan A., Hong W., Lev S.;
RT "Direct interaction between the COG complex and the SM protein, Sly1, is
RT required for Golgi SNARE pairing.";
RL EMBO J. 28:2006-2017(2009).
RN [9]
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 [10]
RP INTERACTION WITH VLDLR, AND SUBCELLULAR LOCATION.
RX PubMed=23701949; DOI=10.1016/j.yexcr.2013.05.010;
RA Wagner T., Dieckmann M., Jaeger S., Weggen S., Pietrzik C.U.;
RT "Stx5 is a novel interactor of VLDL-R to affect its intracellular
RT trafficking and processing.";
RL Exp. Cell Res. 319:1956-1972(2013).
RN [11]
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 [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [13]
RP FUNCTION (MICROBIAL INFECTION), INDUCTION BY HUMAN CYTOMEGALOVIRUS, AND
RP SUBCELLULAR LOCATION.
RX PubMed=27795424; DOI=10.1128/jvi.01637-16;
RA Cruz L., Streck N.T., Ferguson K., Desai T., Desai D.H., Amin S.G.,
RA Buchkovich N.J.;
RT "Potent Inhibition of Human Cytomegalovirus by Modulation of Cellular SNARE
RT Syntaxin 5.";
RL J. Virol. 91:0-0(2017).
RN [14] {ECO:0007744|PDB:3EFO}
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 242-248 IN COMPLEX WITH SEC23A
RP AND SEC24D, INTERACTION WITH SEC24C AND SEC24D, MOTIF, AND MUTAGENESIS OF
RP ILE-245 AND MET-247.
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 [15]
RP VARIANT [LARGE SCALE ANALYSIS] HIS-79.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [16]
RP VARIANT VAL-138.
RX PubMed=29463886; DOI=10.1038/s41380-018-0020-x;
RA Eising E., Carrion-Castillo A., Vino A., Strand E.A., Jakielski K.J.,
RA Scerri T.S., Hildebrand M.S., Webster R., Ma A., Mazoyer B., Francks C.,
RA Bahlo M., Scheffer I.E., Morgan A.T., Shriberg L.D., Fisher S.E.;
RT "A set of regulatory genes co-expressed in embryonic human brain is
RT implicated in disrupted speech development.";
RL Mol. Psychiatry 24:1065-1078(2019).
CC -!- FUNCTION: Mediates endoplasmic reticulum to Golgi transport. Together
CC with p115/USO1 and GM130/GOLGA2, involved in vesicle tethering and
CC fusion at the cis-Golgi membrane to maintain the stacked and inter-
CC connected structure of the Golgi apparatus.
CC {ECO:0000250|UniProtKB:Q08851}.
CC -!- FUNCTION: (Microbial infection) Required for the efficient production
CC of infectious virion during human cytomegalovirus infection.
CC Mechanistically, participates in the formation of the cytoplasmic viral
CC assembly compartment where tegument acquisition and envelopment occur.
CC {ECO:0000269|PubMed:27795424}.
CC -!- SUBUNIT: Part of a ternary complex containing STX5A, NSFL1C and VCP (By
CC similarity). Identified in a unique SNARE complex composed of the Golgi
CC SNAREs GOSR1, GOSR2, YKT6 and VTI1A (By similarity). Interacts with
CC COG4 (PubMed:19536132). Interacts with GM130/GOLGA2 (By similarity).
CC Interacts (via IxM motif) with SEC24C and SEC24D; mediates STX5
CC packaging into COPII-coated vesicles (PubMed:18843296). Interacts with
CC VLDLR; this interaction mediates VLDLR translocation from the
CC endoplasmic reticulum to the plasma membrane (PubMed:23701949).
CC {ECO:0000250|UniProtKB:Q08851, ECO:0000250|UniProtKB:Q8K1E0,
CC ECO:0000269|PubMed:18843296, ECO:0000269|PubMed:19536132,
CC ECO:0000269|PubMed:23701949}.
CC -!- INTERACTION:
CC Q13190; Q4LEZ3: AARD; NbExp=3; IntAct=EBI-714206, EBI-5463075;
CC Q13190; Q06481-5: APLP2; NbExp=3; IntAct=EBI-714206, EBI-25646567;
CC Q13190; Q13520: AQP6; NbExp=3; IntAct=EBI-714206, EBI-13059134;
CC Q13190; Q494R4-2: CCDC153; NbExp=3; IntAct=EBI-714206, EBI-11974185;
CC Q13190; Q9H9E3: COG4; NbExp=2; IntAct=EBI-714206, EBI-368382;
CC Q13190; Q9BUF7-2: CRB3; NbExp=3; IntAct=EBI-714206, EBI-17233035;
CC Q13190; Q68CJ9: CREB3L3; NbExp=3; IntAct=EBI-714206, EBI-852194;
CC Q13190; Q15125: EBP; NbExp=3; IntAct=EBI-714206, EBI-3915253;
CC Q13190; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-714206, EBI-18304435;
CC Q13190; O14653: GOSR2; NbExp=3; IntAct=EBI-714206, EBI-4401517;
CC Q13190; O95872: GPANK1; NbExp=3; IntAct=EBI-714206, EBI-751540;
CC Q13190; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-714206, EBI-13345167;
CC Q13190; Q8NBQ5: HSD17B11; NbExp=3; IntAct=EBI-714206, EBI-1052304;
CC Q13190; Q7Z5P4: HSD17B13; NbExp=3; IntAct=EBI-714206, EBI-18053395;
CC Q13190; Q8N5M9: JAGN1; NbExp=3; IntAct=EBI-714206, EBI-10266796;
CC Q13190; Q8N6L0: KASH5; NbExp=6; IntAct=EBI-714206, EBI-749265;
CC Q13190; Q9HCJ2: LRRC4C; NbExp=3; IntAct=EBI-714206, EBI-3925442;
CC Q13190; P43360: MAGEA6; NbExp=3; IntAct=EBI-714206, EBI-1045155;
CC Q13190; Q9ULD2-3: MTUS1; NbExp=3; IntAct=EBI-714206, EBI-18051665;
CC Q13190; Q9H115: NAPB; NbExp=9; IntAct=EBI-714206, EBI-3921185;
CC Q13190; Q9H6H4: REEP4; NbExp=3; IntAct=EBI-714206, EBI-7545592;
CC Q13190; Q86VR2: RETREG3; NbExp=3; IntAct=EBI-714206, EBI-10192441;
CC Q13190; Q86WV6: STING1; NbExp=3; IntAct=EBI-714206, EBI-2800345;
CC Q13190; Q16623: STX1A; NbExp=3; IntAct=EBI-714206, EBI-712466;
CC Q13190; P32856-2: STX2; NbExp=3; IntAct=EBI-714206, EBI-11956649;
CC Q13190; Q13277: STX3; NbExp=3; IntAct=EBI-714206, EBI-1394295;
CC Q13190; Q12846: STX4; NbExp=6; IntAct=EBI-714206, EBI-744942;
CC Q13190; Q9UNK0: STX8; NbExp=3; IntAct=EBI-714206, EBI-727240;
CC Q13190; P61764: STXBP1; NbExp=6; IntAct=EBI-714206, EBI-960169;
CC Q13190; O75410: TACC1; NbExp=3; IntAct=EBI-714206, EBI-624237;
CC Q13190; O95183: VAMP5; NbExp=4; IntAct=EBI-714206, EBI-10191195;
CC Q13190-4; P05067: APP; NbExp=3; IntAct=EBI-25938350, EBI-77613;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate
CC compartment membrane {ECO:0000250|UniProtKB:Q08851}; Single-pass type
CC IV membrane protein {ECO:0000255}. Golgi apparatus membrane
CC {ECO:0000269|PubMed:27795424}. Note=Localizes throughout the Golgi
CC apparatus, but most abundant in the cis-most cisternae.
CC {ECO:0000269|PubMed:27795424}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing, Alternative initiation; Named isoforms=4;
CC Name=1;
CC IsoId=Q13190-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q13190-2; Sequence=VSP_020119;
CC Name=3;
CC IsoId=Q13190-3; Sequence=VSP_020119, VSP_020120;
CC Name=4;
CC IsoId=Q13190-4; Sequence=VSP_020120;
CC -!- INDUCTION: (Microbial infection) By human cytomegalovirus infection.
CC {ECO:0000269|PubMed:27795424}.
CC -!- MISCELLANEOUS: [Isoform 2]: Produced by alternative initiation at Met-
CC 55 of isoform 1. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: Produced by alternative splicing and
CC alternative initiation. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the syntaxin family. {ECO:0000305}.
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DR EMBL; U26648; AAC71078.1; -; mRNA.
DR EMBL; BX537426; CAD97668.1; -; mRNA.
DR EMBL; AK313497; BAG36279.1; -; mRNA.
DR EMBL; BT019646; AAV38452.1; -; mRNA.
DR EMBL; BT019647; AAV38453.1; -; mRNA.
DR EMBL; AP001160; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002645; AAH02645.1; -; mRNA.
DR EMBL; BC012137; AAH12137.2; -; mRNA.
DR CCDS; CCDS58140.1; -. [Q13190-4]
DR CCDS; CCDS8038.2; -. [Q13190-1]
DR CCDS; CCDS81578.1; -. [Q13190-2]
DR PIR; G01817; G01817.
DR RefSeq; NP_001231595.1; NM_001244666.1. [Q13190-4]
DR RefSeq; NP_001317223.1; NM_001330294.1. [Q13190-2]
DR RefSeq; NP_003155.2; NM_003164.4. [Q13190-1]
DR PDB; 3EFO; X-ray; 2.70 A; C=242-248.
DR PDBsum; 3EFO; -.
DR AlphaFoldDB; Q13190; -.
DR SMR; Q13190; -.
DR BioGRID; 112680; 231.
DR DIP; DIP-56987N; -.
DR IntAct; Q13190; 92.
DR MINT; Q13190; -.
DR STRING; 9606.ENSP00000294179; -.
DR TCDB; 8.A.91.1.9; the syntaxin (syntaxin) family.
DR GlyGen; Q13190; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q13190; -.
DR MetOSite; Q13190; -.
DR PhosphoSitePlus; Q13190; -.
DR BioMuta; STX5; -.
DR DMDM; 114152881; -.
DR EPD; Q13190; -.
DR jPOST; Q13190; -.
DR MassIVE; Q13190; -.
DR MaxQB; Q13190; -.
DR PaxDb; Q13190; -.
DR PeptideAtlas; Q13190; -.
DR PRIDE; Q13190; -.
DR ProteomicsDB; 30190; -.
DR ProteomicsDB; 59212; -. [Q13190-1]
DR ProteomicsDB; 59213; -. [Q13190-2]
DR ProteomicsDB; 59214; -. [Q13190-3]
DR Antibodypedia; 723; 160 antibodies from 29 providers.
DR DNASU; 6811; -.
DR Ensembl; ENST00000294179.8; ENSP00000294179.3; ENSG00000162236.13. [Q13190-1]
DR Ensembl; ENST00000377897.8; ENSP00000367129.4; ENSG00000162236.13. [Q13190-4]
DR Ensembl; ENST00000394690.5; ENSP00000378182.1; ENSG00000162236.13. [Q13190-2]
DR GeneID; 6811; -.
DR KEGG; hsa:6811; -.
DR MANE-Select; ENST00000294179.8; ENSP00000294179.3; NM_003164.5; NP_003155.2.
DR UCSC; uc001nvh.4; human. [Q13190-1]
DR CTD; 6811; -.
DR DisGeNET; 6811; -.
DR GeneCards; STX5; -.
DR HGNC; HGNC:11440; STX5.
DR HPA; ENSG00000162236; Low tissue specificity.
DR MIM; 603189; gene.
DR neXtProt; NX_Q13190; -.
DR OpenTargets; ENSG00000162236; -.
DR PharmGKB; PA36237; -.
DR VEuPathDB; HostDB:ENSG00000162236; -.
DR eggNOG; KOG0812; Eukaryota.
DR GeneTree; ENSGT01000000214440; -.
DR HOGENOM; CLU_044998_1_0_1; -.
DR InParanoid; Q13190; -.
DR OMA; RGITGTM; -.
DR OrthoDB; 1297427at2759; -.
DR PhylomeDB; Q13190; -.
DR TreeFam; TF315068; -.
DR PathwayCommons; Q13190; -.
DR Reactome; R-HSA-204005; COPII-mediated vesicle transport.
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 Reactome; R-HSA-8980692; RHOA GTPase cycle.
DR Reactome; R-HSA-9013106; RHOC GTPase cycle.
DR Reactome; R-HSA-9013408; RHOG GTPase cycle.
DR Reactome; R-HSA-9609523; Insertion of tail-anchored proteins into the endoplasmic reticulum membrane.
DR SignaLink; Q13190; -.
DR SIGNOR; Q13190; -.
DR BioGRID-ORCS; 6811; 466 hits in 1088 CRISPR screens.
DR ChiTaRS; STX5; human.
DR EvolutionaryTrace; Q13190; -.
DR GeneWiki; STX5; -.
DR GenomeRNAi; 6811; -.
DR Pharos; Q13190; Tbio.
DR PRO; PR:Q13190; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q13190; protein.
DR Bgee; ENSG00000162236; Expressed in bone marrow cell and 97 other tissues.
DR ExpressionAtlas; Q13190; baseline and differential.
DR Genevisible; Q13190; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; TAS:Reactome.
DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0031201; C:SNARE complex; IBA:GO_Central.
DR GO; GO:0031982; C:vesicle; IDA:UniProtKB.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
DR GO; GO:0005484; F:SNAP receptor activity; IDA:HGNC-UCL.
DR GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR GO; GO:0034498; P:early endosome to Golgi transport; IMP:UniProtKB.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0090166; P:Golgi disassembly; IDA:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IMP:UniProtKB.
DR GO; GO:1903358; P:regulation of Golgi organization; IDA:UniProtKB.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IDA:HGNC-UCL.
DR GO; GO:0048278; P:vesicle docking; IBA:GO_Central.
DR GO; GO:0006906; P:vesicle fusion; IBA:GO_Central.
DR GO; GO:0048280; P:vesicle fusion with Golgi apparatus; IEA:Ensembl.
DR InterPro; IPR010989; SNARE.
DR InterPro; IPR045242; Syntaxin.
DR InterPro; IPR021538; Syntaxin-5_N.
DR InterPro; IPR006012; Syntaxin/epimorphin_CS.
DR InterPro; IPR000727; T_SNARE_dom.
DR PANTHER; PTHR19957; PTHR19957; 1.
DR Pfam; PF05739; SNARE; 1.
DR Pfam; PF11416; Syntaxin-5_N; 1.
DR SMART; SM00397; t_SNARE; 1.
DR SUPFAM; SSF47661; SSF47661; 1.
DR PROSITE; PS00914; SYNTAXIN; 1.
DR PROSITE; PS50192; T_SNARE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative initiation; Alternative splicing; Coiled coil;
KW Disease variant; Golgi apparatus; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..355
FT /note="Syntaxin-5"
FT /id="PRO_0000210205"
FT TOPO_DOM 1..333
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 334..354
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 355
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT DOMAIN 263..325
FT /note="t-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT REGION 28..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 287..318
FT /evidence="ECO:0000255"
FT MOTIF 245..247
FT /note="IxM motif; signal for cargo packaging into COPII-
FT coated vesicles"
FT /evidence="ECO:0000269|PubMed:18843296"
FT VAR_SEQ 1..54
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:9188044,
FT ECO:0000303|Ref.4"
FT /id="VSP_020119"
FT VAR_SEQ 303..355
FT /note="RIDENVLGAQLDVEAAHSEILKYFQSVTSNRWLMVKIFLILIVFFIIFVVFL
FT A -> SVLLFPLLPALSPGSTRTC (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020120"
FT VARIANT 51
FT /note="P -> L (in dbSNP:rs3802945)"
FT /id="VAR_052248"
FT VARIANT 72
FT /note="Q -> H (in dbSNP:rs11231241)"
FT /id="VAR_052249"
FT VARIANT 79
FT /note="Q -> H (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035642"
FT VARIANT 138
FT /note="I -> V (de novo variant found in a patient with
FT childhood apraxia of speech; unknown pathological
FT significance; dbSNP:rs746774052)"
FT /evidence="ECO:0000269|PubMed:29463886"
FT /id="VAR_081529"
FT MUTAGEN 245
FT /note="I->A: Loss of interaction with SEC24C."
FT /evidence="ECO:0000269|PubMed:18843296"
FT MUTAGEN 247
FT /note="M->A: Loss of interaction with SEC24C."
FT /evidence="ECO:0000269|PubMed:18843296"
FT STRAND 243..246
FT /evidence="ECO:0007829|PDB:3EFO"
SQ SEQUENCE 355 AA; 39673 MW; EE8616A226888501 CRC64;
MIPRKRYGSK NTDQGVYLGL SKTQVLSPAT AGSSSSDIAP LPPPVTLVPP PPDTMSCRDR
TQEFLSACKS LQTRQNGIQT NKPALRAVRQ RSEFTLMAKR IGKDLSNTFA KLEKLTILAK
RKSLFDDKAV EIEELTYIIK QDINSLNKQI AQLQDFVRAK GSQSGRHLQT HSNTIVVSLQ
SKLASMSNDF KSVLEVRTEN LKQQRSRREQ FSRAPVSALP LAPNHLGGGA VVLGAESHAS
KDVAIDMMDS RTSQQLQLID EQDSYIQSRA DTMQNIESTI VELGSIFQQL AHMVKEQEET
IQRIDENVLG AQLDVEAAHS EILKYFQSVT SNRWLMVKIF LILIVFFIIF VVFLA
