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Database: UniProt
Entry: G1PHN1_MYOLU
LinkDB: G1PHN1_MYOLU
Original site: G1PHN1_MYOLU 
ID   G1PHN1_MYOLU            Unreviewed;       355 AA.
AC   G1PHN1;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   SubName: Full=Syntaxin 5 {ECO:0000313|Ensembl:ENSMLUP00000010187.2};
GN   Name=STX5 {ECO:0000313|Ensembl:ENSMLUP00000010187.2};
OS   Myotis lucifugus (Little brown bat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC   Myotis.
OX   NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000010187.2, ECO:0000313|Proteomes:UP000001074};
RN   [1] {ECO:0000313|Ensembl:ENSMLUP00000010187.2, ECO:0000313|Proteomes:UP000001074}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA   Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA   Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA   Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA   Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA   Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA   Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA   Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA   Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA   Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA   Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA   Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA   Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA   Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA   Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSMLUP00000010187.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004211}; Single-
CC       pass type IV membrane protein {ECO:0000256|ARBA:ARBA00004211}.
CC   -!- SIMILARITY: Belongs to the syntaxin family.
CC       {ECO:0000256|ARBA:ARBA00009063}.
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DR   EMBL; AAPE02052745; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_006105929.1; XM_006105867.2.
DR   RefSeq; XP_014303436.1; XM_014447950.1.
DR   AlphaFoldDB; G1PHN1; -.
DR   STRING; 59463.ENSMLUP00000010187; -.
DR   Ensembl; ENSMLUT00000011176.2; ENSMLUP00000010187.2; ENSMLUG00000011176.2.
DR   GeneID; 102432505; -.
DR   KEGG; mlf:102432505; -.
DR   CTD; 6811; -.
DR   eggNOG; KOG0812; Eukaryota.
DR   GeneTree; ENSGT01000000214440; -.
DR   HOGENOM; CLU_044998_1_1_1; -.
DR   InParanoid; G1PHN1; -.
DR   OMA; EHNHNVV; -.
DR   OrthoDB; 70739at2759; -.
DR   TreeFam; TF315068; -.
DR   Proteomes; UP000001074; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:GOC.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031982; C:vesicle; IEA:Ensembl.
DR   GO; GO:0005484; F:SNAP receptor activity; IEA:Ensembl.
DR   GO; GO:0034498; P:early endosome to Golgi transport; IEA:Ensembl.
DR   GO; GO:0090166; P:Golgi disassembly; IEA:Ensembl.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:0045732; P:positive regulation of protein catabolic process; IEA:Ensembl.
DR   GO; GO:1903358; P:regulation of Golgi organization; IEA:Ensembl.
DR   CDD; cd15844; SNARE_syntaxin5; 1.
DR   Gene3D; 1.20.58.70; -; 1.
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; SYNTAXIN; 1.
DR   PANTHER; PTHR19957:SF3; SYNTAXIN-5; 1.
DR   Pfam; PF05739; SNARE; 1.
DR   Pfam; PF11416; Syntaxin-5_N; 1.
DR   SMART; SM00397; t_SNARE; 1.
DR   SUPFAM; SSF47661; t-snare proteins; 1.
DR   PROSITE; PS00914; SYNTAXIN; 1.
DR   PROSITE; PS50192; T_SNARE; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001074};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        334..354
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          263..325
FT                   /note="T-SNARE coiled-coil homology"
FT                   /evidence="ECO:0000259|PROSITE:PS50192"
FT   REGION          27..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          287..314
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   355 AA;  39603 MW;  C97618C5D687FA4C CRC64;
     MIPRKRYGTK NTDQGVYLGL SKTQVLSPAT AGSSSSDIAP PPPPVALVPP PPDTMSCRDR
     TQEFLSACKF LQSRQNGIQT NKPALRAVRQ RSEFSLMAKR IGKDLSNTFA KLEKLTILAK
     RKSLFDDKAV EIEELTYIIK QDINSLNKQI AQLQDFVRAK GSQSGRHLQT HSNTIVVSLQ
     SKLASMSNDF KSVLEVRTEN LKQQRTRREQ FSRAPVSALP LAPNHLGGGA VVLGAESRAS
     GDVAINMLDA RTSQQLQLID EQDSYIQSRA DTMQNIESTI VELGSIFQQL AHMVKEQEET
     IQRIDENVMG AQLDVEGAHS EILKYFQSVT SNRWLMVKIF LILIVFFIIF VVFLA
//
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