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VPS1_SCHPO
ID   VPS1_SCHPO              Reviewed;         678 AA.
AC   Q9URZ5; O14309;
DT   06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2002, sequence version 2.
DT   03-AUG-2022, entry version 135.
DE   RecName: Full=Vacuolar protein sorting-associated protein 1;
GN   Name=vps1; ORFNames=SPAC767.01c, SPAC9G1.14c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
CC   -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC       superfamily. Dynamin/Fzo/YdjA family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01055}.
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DR   EMBL; CU329670; CAB11498.1; -; Genomic_DNA.
DR   PIR; T50256; T50256.
DR   RefSeq; XP_001713062.1; XM_001713010.2.
DR   AlphaFoldDB; Q9URZ5; -.
DR   SMR; Q9URZ5; -.
DR   BioGRID; 279175; 60.
DR   STRING; 4896.SPAC767.01c.1; -.
DR   iPTMnet; Q9URZ5; -.
DR   MaxQB; Q9URZ5; -.
DR   PaxDb; Q9URZ5; -.
DR   PRIDE; Q9URZ5; -.
DR   EnsemblFungi; SPAC767.01c.1; SPAC767.01c.1:pep; SPAC767.01c.
DR   PomBase; SPAC767.01c; vps1.
DR   VEuPathDB; FungiDB:SPAC767.01c; -.
DR   eggNOG; KOG0446; Eukaryota.
DR   HOGENOM; CLU_008964_5_2_1; -.
DR   InParanoid; Q9URZ5; -.
DR   OMA; AMDPTNK; -.
DR   PhylomeDB; Q9URZ5; -.
DR   Reactome; R-SPO-169911; Regulation of Apoptosis.
DR   Reactome; R-SPO-196025; Formation of annular gap junctions.
DR   Reactome; R-SPO-437239; Recycling pathway of L1.
DR   Reactome; R-SPO-75153; Apoptotic execution phase.
DR   Reactome; R-SPO-8856828; Clathrin-mediated endocytosis.
DR   PRO; PR:Q9URZ5; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR   GO; GO:0005794; C:Golgi apparatus; HDA:PomBase.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR   GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR   GO; GO:1990606; F:membrane scission GTPase motor activity; TAS:PomBase.
DR   GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR   GO; GO:0006897; P:endocytosis; ISO:PomBase.
DR   GO; GO:0007031; P:peroxisome organization; IGI:PomBase.
DR   GO; GO:0042144; P:vacuole fusion, non-autophagic; IMP:PomBase.
DR   GO; GO:0099050; P:vesicle scission; NAS:PomBase.
DR   CDD; cd08771; DLP_1; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR022812; Dynamin.
DR   InterPro; IPR001401; Dynamin_GTPase.
DR   InterPro; IPR019762; Dynamin_GTPase_CS.
DR   InterPro; IPR045063; Dynamin_N.
DR   InterPro; IPR000375; Dynamin_stalk.
DR   InterPro; IPR030381; G_DYNAMIN_dom.
DR   InterPro; IPR003130; GED.
DR   InterPro; IPR020850; GED_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR11566; PTHR11566; 1.
DR   Pfam; PF01031; Dynamin_M; 1.
DR   Pfam; PF00350; Dynamin_N; 1.
DR   Pfam; PF02212; GED; 1.
DR   PRINTS; PR00195; DYNAMIN.
DR   SMART; SM00053; DYNc; 1.
DR   SMART; SM00302; GED; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00410; G_DYNAMIN_1; 1.
DR   PROSITE; PS51718; G_DYNAMIN_2; 1.
DR   PROSITE; PS51388; GED; 1.
PE   3: Inferred from homology;
KW   GTP-binding; Motor protein; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..678
FT                   /note="Vacuolar protein sorting-associated protein 1"
FT                   /id="PRO_0000206587"
FT   DOMAIN          24..311
FT                   /note="Dynamin-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   DOMAIN          592..678
FT                   /note="GED"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00720"
FT   REGION          34..41
FT                   /note="G1 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   REGION          60..62
FT                   /note="G2 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   REGION          71..96
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          153..156
FT                   /note="G3 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   REGION          222..225
FT                   /note="G4 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   REGION          252..255
FT                   /note="G5 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   BINDING         34..41
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   BINDING         153..157
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   BINDING         222..225
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   678 AA;  75791 MW;  E2CB9CA2E2F2343B CRC64;
     MDPSLIKVVN QLQEAFSTVG VQNLIDLPQI TVVRSQSSGK SSVLENIVGR DFLPRGTGIV
     TRRPLVLQLI NRPSASGKNE ETTTDSDGKD QNNSSEWGEF LHLPGQKFFE FEKIREEIVR
     ETEEKTGKNV GISSVPIYLR IYSPHVLTLT LVDLPGLTKV PVGDQPRDIE KQIREMVLKY
     ISKNNAIILA VNAANTDLAN SDGLKLAREV DPEGLRTIGV LTKVDLMDKG TDVVDILAGR
     VIPLRLGYVP VINRGQKDIE GKKSIRIALE AERNFFETHP SYGSKAQYCG TPFLARKLNM
     ILMHHIRNTL PEIKVRINAA LAKYQAELHS LGDTPVGDNS SIVLNLITDF CNEYRTVVDG
     RSEELSATEL SGGARIAFVF HEIFSNGIQA IDPFDEVKDS DIRTILYNSS GPSPSLFMGT
     AAFEVIVKQQ IKRLEDPSLK CVSLIYDELV RILNQLLQRP IFKRYPLLKD EFYKVVIGFF
     RKCMQPTNTL VMDMVAMEGS YINTVHPDFL SGHQAMAIVQ SQNSKPIPVD PKTGKALTNN
     PVPPVETSSS SGQNFFGSFF GSKNKKRLAA MEPPPPVLRA STTLSDREKT DTEVIKLLIM
     SYFNIVKRTL ADMVPKSISL KMIKYSKEHI QHELLEQLYK SQAFDKLLQE SEVTVQRRKE
     CEQMVESLLQ ASEIVSNV
 
 
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