STX5_RAT
ID STX5_RAT Reviewed; 355 AA.
AC Q08851; A0JPL4; O55200;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Syntaxin-5;
GN Name=Stx5; Synonyms=Stx5a;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=7690687; DOI=10.1016/0092-8674(93)90466-4;
RA Bennett M.K., Garcia-Arraras J.E., Elferink L.A., Peterson K.E.,
RA Fleming A.M., Hazuka C.D., Scheller R.H.;
RT "The syntaxin family of vesicular transport receptors.";
RL Cell 74:863-873(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Spleen;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-211 (ISOFORM 1), SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND ALTERNATIVE INITIATION.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=9307973; DOI=10.1091/mbc.8.9.1777;
RA Hui N., Nakamura N., Sonnichsen B., Shima D.T., Nilsson T., Warren G.;
RT "An isoform of the Golgi t-SNARE, syntaxin 5, with an endoplasmic reticulum
RT retrieval signal.";
RL Mol. Biol. Cell 8:1777-1787(1997).
RN [4]
RP FUNCTION, AND INTERACTION WITH VCP AND NSFL1C.
RX PubMed=9506515; DOI=10.1016/s0092-8674(00)81128-9;
RA Rabouille C., Kondo H., Newman R., Hui N., Freemont P., Warren G.;
RT "Syntaxin 5 is a common component of the NSF- and p97-mediated reassembly
RT pathways of Golgi cisternae from mitotic Golgi fragments in vitro.";
RL Cell 92:603-610(1998).
RN [5]
RP FUNCTION, AND INTERACTION WITH VCP AND NSFL1C.
RX PubMed=10930451; DOI=10.1091/mbc.11.8.2529;
RA Roy L., Bergeron J.J.M., Lavoie C., Hendriks R., Gushue J., Fazel A.,
RA Pelletier A., Morre D.J., Subramaniam V.N., Hong W., Paiement J.;
RT "Role of p97 and syntaxin 5 in the assembly of transitional endoplasmic
RT reticulum.";
RL Mol. Biol. Cell 11:2529-2542(2000).
RN [6]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH GOSR1; GOSR2 AND YKT6.
RX PubMed=11323436; DOI=10.1074/jbc.m102786200;
RA Zhang T., Hong W.;
RT "Ykt6 forms a SNARE complex with syntaxin 5, GS28, and Bet1 and
RT participates in a late stage in endoplasmic reticulum-Golgi transport.";
RL J. Biol. Chem. 276:27480-27487(2001).
RN [7]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=14742712; DOI=10.1091/mbc.e03-08-0625;
RA Volchuk A., Ravazzola M., Perrelet A., Eng W.S., Di Liberto M.,
RA Varlamov O., Fukasawa M., Engel T., Sollner T.H., Rothman J.E., Orci L.;
RT "Countercurrent distribution of two distinct SNARE complexes mediating
RT transport within the Golgi stack.";
RL Mol. Biol. Cell 15:1506-1518(2004).
RN [8]
RP FUNCTION, AND INTERACTION WITH GOLGA2.
RX PubMed=18167358; DOI=10.1074/jbc.m708401200;
RA Diao A., Frost L., Morohashi Y., Lowe M.;
RT "Coordination of golgin tethering and SNARE assembly: GM130 binds syntaxin
RT 5 in a p115-regulated manner.";
RL J. Biol. Chem. 283:6957-6967(2008).
CC -!- FUNCTION: Mediates endoplasmic reticulum to Golgi transport
CC (PubMed:10930451, PubMed:14742712, PubMed:9506515). Together with
CC p115/USO1 and GM130/GOLGA2, involved in vesicle tethering and fusion at
CC the cis-Golgi membrane to maintain the stacked and inter-connected
CC structure of the Golgi apparatus (PubMed:18167358).
CC {ECO:0000269|PubMed:10930451, ECO:0000269|PubMed:14742712,
CC ECO:0000269|PubMed:18167358, ECO:0000269|PubMed:9506515}.
CC -!- SUBUNIT: Part of a ternary complex containing STX5A, NSFL1C and VCP
CC (PubMed:9506515). Part of a unique SNARE complex composed of the Golgi
CC SNAREs GOSR1, GOSR2 and YKT6. This complex also includes VTI1A (By
CC similarity). Interacts with COG4 (By similarity). Interacts with
CC GM130/GOLGA2 (PubMed:18167358). Interacts (via IxM motif) with SEC24C
CC and SEC24D; mediates STX5 packaging into COPII-coated vesicles (By
CC similarity). Interacts with VLDLR; this interaction mediates VLDLR
CC translocation from the endoplasmic reticulum to the plasma membrane (By
CC similarity). {ECO:0000250|UniProtKB:Q13190,
CC ECO:0000250|UniProtKB:Q8K1E0, ECO:0000269|PubMed:18167358,
CC ECO:0000269|PubMed:9506515}.
CC -!- INTERACTION:
CC Q08851; Q62931: Gosr1; NbExp=15; IntAct=EBI-2028244, EBI-7837133;
CC Q08851; P41542: Uso1; NbExp=8; IntAct=EBI-2028244, EBI-4423297;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate
CC compartment membrane {ECO:0000269|PubMed:11323436,
CC ECO:0000269|PubMed:9307973}; Single-pass type IV membrane protein
CC {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:9307973}.
CC Note=Localizes throughout the Golgi apparatus, but most abundant in the
CC cis-most cisternae. {ECO:0000269|PubMed:9307973}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=1;
CC IsoId=Q08851-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q08851-2; Sequence=VSP_020117;
CC -!- TISSUE SPECIFICITY: Expressed in the brain, heart, spleen, lung, liver,
CC kidney and testis. {ECO:0000269|PubMed:9307973}.
CC -!- MISCELLANEOUS: [Isoform 2]: Produced by alternative initiation at Met-
CC 55 of isoform 1. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the syntaxin 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; L20822; AAA03047.1; -; mRNA.
DR EMBL; BC127489; AAI27490.1; -; mRNA.
DR EMBL; U87971; AAB93844.1; -; mRNA.
DR PIR; F48213; F48213.
DR RefSeq; NP_113892.2; NM_031704.2. [Q08851-1]
DR RefSeq; XP_006231059.1; XM_006230997.2. [Q08851-1]
DR AlphaFoldDB; Q08851; -.
DR SMR; Q08851; -.
DR BioGRID; 249255; 2.
DR CORUM; Q08851; -.
DR IntAct; Q08851; 11.
DR STRING; 10116.ENSRNOP00000025664; -.
DR PhosphoSitePlus; Q08851; -.
DR jPOST; Q08851; -.
DR PaxDb; Q08851; -.
DR PRIDE; Q08851; -.
DR Ensembl; ENSRNOT00000095404; ENSRNOP00000092180; ENSRNOG00000018847. [Q08851-1]
DR GeneID; 65134; -.
DR KEGG; rno:65134; -.
DR UCSC; RGD:68426; rat. [Q08851-1]
DR CTD; 6811; -.
DR RGD; 68426; Stx5.
DR eggNOG; KOG0812; Eukaryota.
DR GeneTree; ENSGT01000000214440; -.
DR HOGENOM; CLU_044998_1_1_1; -.
DR InParanoid; Q08851; -.
DR OMA; RGITGTM; -.
DR OrthoDB; 1297427at2759; -.
DR PhylomeDB; Q08851; -.
DR TreeFam; TF315068; -.
DR Reactome; R-RNO-204005; COPII-mediated vesicle transport.
DR Reactome; R-RNO-5694530; Cargo concentration in the ER.
DR Reactome; R-RNO-6807878; COPI-mediated anterograde transport.
DR Reactome; R-RNO-6811438; Intra-Golgi traffic.
DR Reactome; R-RNO-8980692; RHOA GTPase cycle.
DR Reactome; R-RNO-9013106; RHOC GTPase cycle.
DR Reactome; R-RNO-9013408; RHOG GTPase cycle.
DR Reactome; R-RNO-9609523; Insertion of tail-anchored proteins into the endoplasmic reticulum membrane.
DR PRO; PR:Q08851; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000018847; Expressed in pancreas and 20 other tissues.
DR Genevisible; Q08851; RN.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:RGD.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR GO; GO:0000139; C:Golgi membrane; IDA:RGD.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0031201; C:SNARE complex; IDA:RGD.
DR GO; GO:0031982; C:vesicle; ISO:RGD.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:RGD.
DR GO; GO:0005484; F:SNAP receptor activity; ISO:RGD.
DR GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR GO; GO:0034498; P:early endosome to Golgi transport; ISO:RGD.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IDA:RGD.
DR GO; GO:0090166; P:Golgi disassembly; ISO:RGD.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; ISO:RGD.
DR GO; GO:1903358; P:regulation of Golgi organization; ISO:RGD.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISO:RGD.
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; IDA:RGD.
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 Alternative initiation; Coiled coil; Golgi apparatus; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..355
FT /note="Syntaxin-5"
FT /id="PRO_0000210207"
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 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:0000250|UniProtKB:Q13190"
FT VAR_SEQ 1..54
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7690687"
FT /id="VSP_020117"
SQ SEQUENCE 355 AA; 39751 MW; 0B0D0B2C261A39B4 CRC64;
MIPRKRYGSK NTDQGVYLGL SKTQVLSPAT AINSSSDIAP LPTPVALVPS PPDTMSCRDR
TQEFLSACKS LQSRQNGIQT NKPALHATRQ CSEFTLMARR IGKDLSNTFA KLEKLTILAK
RKSLFDDKAV EIEELTYIIK QDINSLNKQI AQLQDFVRAK GSQSGRHLQT HSNTIVVSLQ
SKLASMSNDF KSVLEVRTEN LKQQRNRREQ FSRAPVSALP LAPNNLGGGP IVLGGESRAS
RDVAIDMMDP RTSQQLQLID EQDSYIQSRA DTMQNIESTI VELGSIFQQL AHMVKEQEET
IQRIDENVLG AQLDVEAAHS EILKYFQSVT SNRWLMVKIF LILIVFFIIF VVFLA
