ID A0A016RUK1_9BILA Unreviewed; 443 AA.
AC A0A016RUK1;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=t-SNARE coiled-coil homology domain-containing protein {ECO:0000259|PROSITE:PS50192};
GN Name=Acey_s0373.g164 {ECO:0000313|EMBL:EYB81802.1};
GN Synonyms=Acey-syx-5 {ECO:0000313|EMBL:EYB81802.1};
GN ORFNames=Y032_0373g164 {ECO:0000313|EMBL:EYB81802.1};
OS Ancylostoma ceylanicum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=53326 {ECO:0000313|EMBL:EYB81802.1, ECO:0000313|Proteomes:UP000024635};
RN [1] {ECO:0000313|Proteomes:UP000024635}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX PubMed=25730766; DOI=10.1038/ng.3237;
RA Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA Aroian R.V.;
RT "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT ceylanicum identify infection-specific gene families.";
RL Nat. Genet. 47:416-422(2015).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EYB81802.1}.
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DR EMBL; JARK01001709; EYB81802.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A016RUK1; -.
DR STRING; 53326.A0A016RUK1; -.
DR Proteomes; UP000024635; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005484; F:SNAP receptor activity; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0006836; P:neurotransmitter transport; IEA:UniProtKB-KW.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Neurotransmitter transport {ECO:0000256|ARBA:ARBA00022775};
KW Reference proteome {ECO:0000313|Proteomes:UP000024635};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022775}.
FT TRANSMEM 422..442
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 351..413
FT /note="T-SNARE coiled-coil homology"
FT /evidence="ECO:0000259|PROSITE:PS50192"
FT REGION 36..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 280..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..294
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 443 AA; 49545 MW; 7E023C2434308A6E CRC64;
MPSRQVPRRR TTVTAEDVSY ATTVCSCRMS DFSVRSRRRV EDSKPPVTAF EDHDAKKESA
SVPSSIFGNY SSLSSTVFGA SPTQLWNSAQ EAFSSIPSTL YYPPEQSAPQ EFVEKDFPAL
SIFGDPVDSF TFTMPSRDRT AEFRTTCKSL QMKVHSNGFI QPTKKEILND SVQFNQLAKR
IGRDLSQTCA KMEKLAEMAK KKSLFDEKSD MDHLSRIVKE DITGLNKQIA ALQEFSRRRS
GGAKNQGTGH TQLVVVGLQS KLASVSKDFQ SVLEISTENL KHQKSRREKF SHADHVPMSL
PSSSSGSNVR SRLLEDDNQH GVPRVSSVSL DMGAMEQMRA QQQMTLQDQS DTYAQARSNA
METIEGSISE LGQIFAQLAS LVSEQGEMIT RIDSNVEDTA INIDAAHTEL VKYFHNISKN
RWLMIKVFGV LMVFFIIFVL FLT
//