ID   STX7_PONAB              Reviewed;         261 AA.
AC   Q5R602;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Syntaxin-7;
GN   Name=STX7;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May be involved in protein trafficking from the plasma
CC       membrane to the early endosome (EE) as well as in homotypic fusion of
CC       endocytic organelles. Mediates the endocytic trafficking from early
CC       endosomes to late endosomes and lysosomes (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Forms a SNARE complex with VTI1B, STX8 and VAMP8 which
CC       functions in the homotypic fusion of late endosomes. Component of the
CC       SNARE complex composed of STX7, STX8, VAMP7 and VTI1B that is required
CC       for heterotypic fusion of late endosomes with lysosomes. Interacts with
CC       VPS11, VPS16 and VPS18. Interacts with VPS33A (By similarity).
CC       Interacts with TPC1 (By similarity). {ECO:0000250,
CC       ECO:0000250|UniProtKB:O70439}.
CC   -!- SUBCELLULAR LOCATION: Early endosome membrane {ECO:0000250}; Single-
CC       pass type IV membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the syntaxin family. {ECO:0000305}.
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DR   EMBL; CR860698; CAH92814.1; -; mRNA.
DR   RefSeq; NP_001127590.1; NM_001134118.1.
DR   AlphaFoldDB; Q5R602; -.
DR   SMR; Q5R602; -.
DR   STRING; 9601.ENSPPYP00000019051; -.
DR   GeneID; 100174669; -.
DR   KEGG; pon:100174669; -.
DR   CTD; 8417; -.
DR   eggNOG; KOG0811; Eukaryota.
DR   InParanoid; Q5R602; -.
DR   OrthoDB; 1204812at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005484; F:SNAP receptor activity; IEA:InterPro.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR   CDD; cd00179; SynN; 1.
DR   InterPro; IPR010989; SNARE.
DR   InterPro; IPR045242; Syntaxin.
DR   InterPro; IPR006012; Syntaxin/epimorphin_CS.
DR   InterPro; IPR006011; Syntaxin_N.
DR   InterPro; IPR000727; T_SNARE_dom.
DR   PANTHER; PTHR19957; PTHR19957; 1.
DR   Pfam; PF05739; SNARE; 1.
DR   Pfam; PF14523; Syntaxin_2; 1.
DR   SMART; SM00503; SynN; 1.
DR   SMART; SM00397; t_SNARE; 1.
DR   SUPFAM; SSF47661; SSF47661; 1.
DR   PROSITE; PS00914; SYNTAXIN; 1.
DR   PROSITE; PS50192; T_SNARE; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Coiled coil; Endosome; Membrane; Phosphoprotein;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:O15400"
FT   CHAIN           2..261
FT                   /note="Syntaxin-7"
FT                   /id="PRO_0000210215"
FT   TOPO_DOM        2..238
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        239..259
FT                   /note="Helical; Anchor for type IV membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        260..261
FT                   /note="Vesicular"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          165..227
FT                   /note="t-SNARE coiled-coil homology"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT   REGION          129..148
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          47..69
FT                   /evidence="ECO:0000255"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:O15400"
FT   MOD_RES         4
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O15400"
FT   MOD_RES         45
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O15400"
FT   MOD_RES         75
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O15400"
FT   MOD_RES         79
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O70439"
FT   MOD_RES         125
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O70439"
FT   MOD_RES         126
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O15400"
FT   MOD_RES         129
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O15400"
FT   MOD_RES         205
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O15400"
SQ   SEQUENCE   261 AA;  29821 MW;  14B5B693FCC80D10 CRC64;
     MSYTPGVGGD PAQLAQRISS NIQKITQCSA EIQRTLNQLG TPQDSPELRQ QLQQKQQYTN
     QLTKETDKYI KEFGSLPTTP SEQRQRKIQK DRLVGEFTTS LTNFQKVQRQ AAEREKEFVA
     RVRASSRVSG SFPEDSSKER NLVSWESQTQ PQVQVQDEEI TEDDLRLIHE RESSIRQLEA
     DIMDINEIFK DLGMMIHEQG DVIDSIEANV ENAEVHVQQA NQQLSRAADY QRKSRKTLCI
     IILILVIGVV IIGLIIWGLN R