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VTI1A_DICDI
ID   VTI1A_DICDI             Reviewed;         217 AA.
AC   Q54CK6;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=Vesicle transport through interaction with t-SNAREs homolog 1A;
GN   Name=vti1A {ECO:0000312|EMBL:EAL61036.1};
GN   Synonyms=vti1 {ECO:0000312|dictyBase:DDB_G0292974}; ORFNames=DDB_G0292974;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1] {ECO:0000312|EMBL:EAL61036.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 39-49, FUNCTION, IDENTIFICATION IN SNARE COMPLEX, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=12175335; DOI=10.1042/bj20020845;
RA   Bogdanovic A., Bennett N., Kieffer S., Louwagie M., Morio T., Garin J.,
RA   Satre M., Bruckert F.;
RT   "Syntaxin 7, syntaxin 8, Vti1 and VAMP7 (vesicle-associated membrane
RT   protein 7) form an active SNARE complex for early macropinocytic
RT   compartment fusion in Dictyostelium discoideum.";
RL   Biochem. J. 368:29-39(2002).
RN   [3] {ECO:0000305}
RP   DEVELOPMENTAL STAGE.
RX   PubMed=11923193; DOI=10.1242/dev.129.7.1543;
RA   Van Driessche N., Shaw C., Katoh M., Morio T., Sucgang R., Ibarra M.,
RA   Kuwayama H., Saito T., Urushihara H., Maeda M., Takeuchi I., Ochiai H.,
RA   Eaton W., Tollett J., Halter J., Kuspa A., Tanaka Y., Shaulsky G.;
RT   "A transcriptional profile of multicellular development in Dictyostelium
RT   discoideum.";
RL   Development 129:1543-1552(2002).
CC   -!- FUNCTION: V-SNARE that mediates vesicle transport pathways through
CC       interactions with t-SNAREs on the target membrane. These interactions
CC       are proposed to mediate aspects of the specificity of vesicle
CC       trafficking and to promote fusion of the lipid bilayers.
CC       {ECO:0000250|UniProtKB:Q9JI51, ECO:0000269|PubMed:12175335}.
CC   -!- SUBUNIT: Component of the SNARE complex composed of syn7A, syn8A,
CC       vamp7A and vti1A. {ECO:0000269|PubMed:12175335}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:12175335}; Single-
CC       pass type IV membrane protein {ECO:0000269|PubMed:12175335}.
CC       Cytoplasmic vesicle, secretory vesicle membrane
CC       {ECO:0000269|PubMed:12175335}; Single-pass type IV membrane protein
CC       {ECO:0000269|PubMed:12175335}. Cytoplasmic vesicle, clathrin-coated
CC       vesicle membrane {ECO:0000250|UniProtKB:Q9JI51, ECO:0000255}; Single-
CC       pass type IV membrane protein {ECO:0000250|UniProtKB:Q9JI51,
CC       ECO:0000255}. Endosome membrane {ECO:0000269|PubMed:12175335}; Single-
CC       pass type IV membrane protein {ECO:0000269|PubMed:12175335}.
CC       Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type IV
CC       membrane protein {ECO:0000250|UniProtKB:Q9JI51, ECO:0000255}.
CC   -!- DEVELOPMENTAL STAGE: Expressed during development. Expression levels
CC       peak at 2 hours, after which they decrease steadily until culmination.
CC       Levels increase after 18 hours of development.
CC       {ECO:0000269|PubMed:11923193}.
CC   -!- SIMILARITY: Belongs to the VTI1 family. {ECO:0000255}.
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DR   EMBL; AAFI02000197; EAL61036.1; -; Genomic_DNA.
DR   RefSeq; XP_629410.1; XM_629408.1.
DR   AlphaFoldDB; Q54CK6; -.
DR   SMR; Q54CK6; -.
DR   IntAct; Q54CK6; 1.
DR   STRING; 44689.DDB0231536; -.
DR   PaxDb; Q54CK6; -.
DR   EnsemblProtists; EAL61036; EAL61036; DDB_G0292974.
DR   GeneID; 8628929; -.
DR   KEGG; ddi:DDB_G0292974; -.
DR   dictyBase; DDB_G0292974; vti1A.
DR   eggNOG; KOG1666; Eukaryota.
DR   HOGENOM; CLU_075474_0_1_1; -.
DR   InParanoid; Q54CK6; -.
DR   OMA; KLRMYRR; -.
DR   PhylomeDB; Q54CK6; -.
DR   Reactome; R-DDI-6811438; Intra-Golgi traffic.
DR   Reactome; R-DDI-6811440; Retrograde transport at the Trans-Golgi-Network.
DR   PRO; PR:Q54CK6; -.
DR   Proteomes; UP000002195; Chromosome 6.
DR   GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000331; C:contractile vacuole; IDA:dictyBase.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR   GO; GO:0005768; C:endosome; IDA:dictyBase.
DR   GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
DR   GO; GO:0012507; C:ER to Golgi transport vesicle membrane; IBA:GO_Central.
DR   GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031902; C:late endosome membrane; IBA:GO_Central.
DR   GO; GO:0045335; C:phagocytic vesicle; IDA:dictyBase.
DR   GO; GO:0032010; C:phagolysosome; IDA:dictyBase.
DR   GO; GO:0031201; C:SNARE complex; IDA:dictyBase.
DR   GO; GO:0005484; F:SNAP receptor activity; IBA:GO_Central.
DR   GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:0006906; P:vesicle fusion; IDA:UniProtKB.
DR   GO; GO:0016192; P:vesicle-mediated transport; IDA:UniProtKB.
DR   Gene3D; 1.20.58.400; -; 1.
DR   InterPro; IPR010989; SNARE.
DR   InterPro; IPR000727; T_SNARE_dom.
DR   InterPro; IPR038407; v-SNARE_N_sf.
DR   InterPro; IPR007705; Vesicle_trsprt_v-SNARE_N.
DR   Pfam; PF05008; V-SNARE; 1.
DR   SMART; SM00397; t_SNARE; 1.
DR   SUPFAM; SSF47661; SSF47661; 1.
DR   PROSITE; PS50192; T_SNARE; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Cytoplasmic vesicle; Direct protein sequencing;
KW   Endoplasmic reticulum; Endosome; Membrane; Protein transport;
KW   Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..217
FT                   /note="Vesicle transport through interaction with t-SNAREs
FT                   homolog 1A"
FT                   /id="PRO_0000319996"
FT   TOPO_DOM        1..192
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9JI51, ECO:0000255"
FT   TRANSMEM        193..213
FT                   /note="Helical; Anchor for type IV membrane protein"
FT   TOPO_DOM        214..217
FT                   /note="Vesicular"
FT                   /evidence="ECO:0000250|UniProtKB:Q9JI51, ECO:0000255"
FT   DOMAIN          123..185
FT                   /note="t-SNARE coiled-coil homology"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT   REGION          90..109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          36..97
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   217 AA;  25225 MW;  2C41B7DF05B6B7D3 CRC64;
     MDVFERTEQN FQHVCNSITR RIKQLPNYGG EKKKIAVREV ENDIDEALKF ISEMEKLAQN
     HPQRIKLQTK TKQYHSDIQK YKREVQLAQL QSSNQTNSNP WSNAPDDYQS QYDNQRQHLL
     QGSNMLDSTS DRLLRTHQIS AQSEQIGQNI LMDLGKQGEQ IRGMRDKLHE TDDQIKSARK
     IMTGIARRLA TNKVILSIII LLLMGIIALI ICLKWLR
 
 
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