STX5_MOUSE
ID STX5_MOUSE Reviewed; 355 AA.
AC Q8K1E0; Q3TM79; Q99J28; Q9JKP2;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 3.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Syntaxin-5;
GN Name=Stx5; Synonyms=Stx5a;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Low D.Y.H., Tang B.L., Hong W.;
RT "Mouse syntaxin 5.";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Lung;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N-3; TISSUE=Mammary gland;
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 [4]
RP IDENTIFICATION IN SNARE COMPLEX WITH VTI1A, AND SUBCELLULAR LOCATION.
RX PubMed=9705316; DOI=10.1074/jbc.273.34.21783;
RA Xu Y., Wong S.H., Tang B.L., Subramaniam V.N., Zhang T., Hong W.;
RT "A 29-kilodalton Golgi soluble N-ethylmaleimide-sensitive factor attachment
RT protein receptor (Vti1-rp2) implicated in protein trafficking in the
RT secretory pathway.";
RL J. Biol. Chem. 273:21783-21789(1998).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 -!- SUBUNIT: Part of a ternary complex containing STX5A, NSFL1C and VCP.
CC Part of a unique SNARE complex composed of the Golgi SNAREs GOSR1,
CC GOSR2, YKT6 and VTI1A (PubMed:9705316). Interacts with COG4 (By
CC similarity). Interacts with GM130/GOLGA2 (By similarity). Interacts
CC (via IxM motif) with SEC24C and SEC24D; mediates STX5 packaging into
CC COPII-coated vesicles (By similarity). Interacts with VLDLR; this
CC interaction mediates VLDLR translocation from the endoplasmic reticulum
CC to the plasma membrane (By similarity). {ECO:0000250|UniProtKB:Q08851,
CC ECO:0000250|UniProtKB:Q13190, ECO:0000269|PubMed:9705316}.
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:0000250|UniProtKB:Q08851}. Note=Localizes throughout the Golgi
CC apparatus, but most abundant in the cis-most cisternae.
CC {ECO:0000250|UniProtKB:Q08851}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=1;
CC IsoId=Q8K1E0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8K1E0-2; Sequence=VSP_020118;
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 -!- CAUTION: It is uncertain whether Met-1 or Met-55 is the initiator.
CC However, for the rat ortholog it has been shown that the equivalent
CC alternative isoform is produced by alternative initiation at a
CC conserved initiator methionine at position 55. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH04849.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH21883.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF232709; AAF36981.1; -; mRNA.
DR EMBL; AK166087; BAE38563.1; -; mRNA.
DR EMBL; BC004849; AAH04849.1; ALT_INIT; mRNA.
DR EMBL; BC021883; AAH21883.1; ALT_INIT; mRNA.
DR CCDS; CCDS29542.2; -. [Q8K1E0-1]
DR RefSeq; NP_001161271.1; NM_001167799.1. [Q8K1E0-1]
DR RefSeq; NP_062803.4; NM_019829.4. [Q8K1E0-1]
DR AlphaFoldDB; Q8K1E0; -.
DR SMR; Q8K1E0; -.
DR BioGRID; 207947; 1.
DR STRING; 10090.ENSMUSP00000134854; -.
DR iPTMnet; Q8K1E0; -.
DR PhosphoSitePlus; Q8K1E0; -.
DR SwissPalm; Q8K1E0; -.
DR EPD; Q8K1E0; -.
DR jPOST; Q8K1E0; -.
DR MaxQB; Q8K1E0; -.
DR PaxDb; Q8K1E0; -.
DR PeptideAtlas; Q8K1E0; -.
DR PRIDE; Q8K1E0; -.
DR Antibodypedia; 723; 160 antibodies from 29 providers.
DR DNASU; 56389; -.
DR Ensembl; ENSMUST00000073430; ENSMUSP00000073136; ENSMUSG00000010110. [Q8K1E0-1]
DR Ensembl; ENSMUST00000176381; ENSMUSP00000134854; ENSMUSG00000010110. [Q8K1E0-1]
DR GeneID; 56389; -.
DR KEGG; mmu:56389; -.
DR UCSC; uc008gmo.2; mouse. [Q8K1E0-1]
DR CTD; 56389; -.
DR MGI; MGI:1928483; Stx5a.
DR VEuPathDB; HostDB:ENSMUSG00000010110; -.
DR eggNOG; KOG0812; Eukaryota.
DR GeneTree; ENSGT01000000214440; -.
DR HOGENOM; CLU_044998_0_1_1; -.
DR InParanoid; Q8K1E0; -.
DR OMA; RGITGTM; -.
DR OrthoDB; 1297427at2759; -.
DR PhylomeDB; Q8K1E0; -.
DR TreeFam; TF315068; -.
DR Reactome; R-MMU-204005; COPII-mediated vesicle transport.
DR Reactome; R-MMU-5694530; Cargo concentration in the ER.
DR Reactome; R-MMU-6807878; COPI-mediated anterograde transport.
DR Reactome; R-MMU-6811438; Intra-Golgi traffic.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013106; RHOC GTPase cycle.
DR Reactome; R-MMU-9013408; RHOG GTPase cycle.
DR Reactome; R-MMU-9609523; Insertion of tail-anchored proteins into the endoplasmic reticulum membrane.
DR BioGRID-ORCS; 56389; 27 hits in 76 CRISPR screens.
DR ChiTaRS; Stx5a; mouse.
DR PRO; PR:Q8K1E0; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q8K1E0; protein.
DR Bgee; ENSMUSG00000010110; Expressed in primary oocyte and 260 other tissues.
DR ExpressionAtlas; Q8K1E0; baseline and differential.
DR Genevisible; Q8K1E0; MM.
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; ISO:MGI.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0000139; C:Golgi membrane; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0031201; C:SNARE complex; ISO:MGI.
DR GO; GO:0031982; C:vesicle; ISO:MGI.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
DR GO; GO:0005484; F:SNAP receptor activity; ISO:MGI.
DR GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR GO; GO:0034498; P:early endosome to Golgi transport; ISO:MGI.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; ISO:MGI.
DR GO; GO:0090166; P:Golgi disassembly; ISO:MGI.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; ISO:MGI.
DR GO; GO:1903358; P:regulation of Golgi organization; ISO:MGI.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0016192; P:vesicle-mediated transport; TAS:MGI.
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_0000210206"
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:16141072, ECO:0000303|Ref.1"
FT /id="VSP_020118"
FT CONFLICT 91
FT /note="C -> S (in Ref. 3; AAH21883)"
FT /evidence="ECO:0000305"
FT CONFLICT 179..180
FT /note="LQ -> FE (in Ref. 1; AAF36981)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 355 AA; 39713 MW; 29CFD4EA5665CFEF CRC64;
MIPRKRYGSK NTDQGVYLGL SKTQVLSPAT AISSSSDSTP LPTPVALVPS PPDTMSCRDR
TQEFQSACKS LQSRQNGIQT SKPALHAARQ CSEFTLMARR IGKDLSNTFA KLEKLTILAK
RKSLFDDKAV EIEELTYIIK QDINSLNKQI AQLQDFVRAK GSQSGRHLQT HSNTIVVSLQ
SKLASMSNDF KSVLEVRTEN LKQQRNRREQ FSRAPVSALP LAPNNLGGGP IILGAESRAS
RDVAIDMMDP RTSQQLQLID EQDSYIQSRA DTMQNIESTI VELGSIFQQL AHMVKEQEET
IQRIDENVLG AQLDVEAAHS EILKYFQSVT SNRWLMVKIF LILIVFFIIF VVFLA
