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VMS1_SCHPO
ID   VMS1_SCHPO              Reviewed;         600 AA.
AC   O74977;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=VMS1 homolog C1827.04;
GN   ORFNames=SPCC1827.04;
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).
RN   [2]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RX   PubMed=18257517; DOI=10.1021/pr7006335;
RA   Wilson-Grady J.T., Villen J., Gygi S.P.;
RT   "Phosphoproteome analysis of fission yeast.";
RL   J. Proteome Res. 7:1088-1097(2008).
CC   -!- FUNCTION: Involved in the endoplasmic reticulum (ER)-associated
CC       degradation (ERAD) pathway. Component of an evolutionarily conserved
CC       system for ubiquitin-mediated mitochondria-associated protein
CC       degradation (MAD), which is necessary to maintain mitochondrial,
CC       cellular, and organismal viability (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC       Mitochondrion {ECO:0000250}. Endoplasmic reticulum membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ANKZF1/VMS1 family. {ECO:0000305}.
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DR   EMBL; CU329672; CAA19312.1; -; Genomic_DNA.
DR   PIR; T41165; T41165.
DR   RefSeq; NP_588550.1; NM_001023537.2.
DR   AlphaFoldDB; O74977; -.
DR   SMR; O74977; -.
DR   BioGRID; 275759; 27.
DR   STRING; 4896.SPCC1827.04.1; -.
DR   iPTMnet; O74977; -.
DR   MaxQB; O74977; -.
DR   PaxDb; O74977; -.
DR   PRIDE; O74977; -.
DR   EnsemblFungi; SPCC1827.04.1; SPCC1827.04.1:pep; SPCC1827.04.
DR   PomBase; SPCC1827.04; -.
DR   VEuPathDB; FungiDB:SPCC1827.04; -.
DR   eggNOG; KOG2505; Eukaryota.
DR   HOGENOM; CLU_014293_1_1_1; -.
DR   InParanoid; O74977; -.
DR   OMA; QKTIHRY; -.
DR   PhylomeDB; O74977; -.
DR   PRO; PR:O74977; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0036266; C:Cdc48p-Npl4p-Vms1p AAA ATPase complex; ISO:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:PomBase.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISO:PomBase.
DR   Gene3D; 1.25.40.20; -; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR041175; VLRF1/Vms1.
DR   Pfam; PF13857; Ank_5; 1.
DR   Pfam; PF18826; bVLRF1; 1.
DR   SMART; SM00248; ANK; 1.
DR   SUPFAM; SSF48403; SSF48403; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 1.
PE   1: Evidence at protein level;
KW   ANK repeat; Coiled coil; Cytoplasm; Endoplasmic reticulum; Membrane;
KW   Mitochondrion; Phosphoprotein; Reference proteome; Repeat.
FT   CHAIN           1..600
FT                   /note="VMS1 homolog C1827.04"
FT                   /id="PRO_0000310323"
FT   REPEAT          432..461
FT                   /note="ANK 1"
FT   REPEAT          465..492
FT                   /note="ANK 2"
FT   REGION          239..263
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          517..563
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          359..392
FT                   /evidence="ECO:0000255"
FT   COILED          506..550
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        242..261
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        517..558
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         38
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   600 AA;  68793 MW;  5FA84FA561153037 CRC64;
     MGDISKHNIF SLPEDILAKL ELREEYSVEE KTDSANLSNQ GDIVDSTQKN ISSCVNCQID
     NLHTLDERKS HIKSDWHRFN TKRKITKLPP VSQDEFESII EDLPESLSGS ESETNSESEE
     DNFQIEKAFK QSLNIGKVDS ADENNNQRTN SPLTWFQLSN ASAEVPTYIG VYKHMFSGNN
     HITKDLLVQQ QNHNRQKPLQ LAMFMVGGGH FAAMIASNEF NPRDPHVPKV LAQKTIHRYT
     TRRKQGGSQG AADNTKGNIH SAGSGLRRYN EQALIKDIQQ VFKDWGKLLE TCDLIFVRAI
     GSSNRSIFFS QPGALISPKD PKLRVFPFTT KRATHSELLR CYKELVTPKI SHVDSISIKA
     QEEERKRQAE IEKEIRQSRL QEEERKKKKL AKYTEVIISN LKASNIEAFL EYLRSNDLSI
     NFQFYPKNVH LHTSTPLHYA VTQKNAKLVA KLLRNGADPA MLNGNGKTPF EISTGNKEVK
     DEFLIARHEL GESFFDWEAA KVGAPQSREQ IQKQRQKAKT KLENQRRDKE RQEELRRKEA
     MQKIEEQSKR DYDKLHGEGH SLGINNVRKV DELQSLSPEM RMRIEREKRA AAAMKRMQTK
 
 
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