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VTC2_SCHPO
ID   VTC2_SCHPO              Reviewed;         734 AA.
AC   O13718;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 124.
DE   RecName: Full=Vacuolar transporter chaperone 2;
GN   Name=vtc2; ORFNames=SPAC14C4.11;
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181; THR-529 AND TYR-583, AND
RP   IDENTIFICATION BY 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: Component of the vacuolar transporter chaperone (VTC)
CC       complex, which plays a role in vacuolar membrane fusion. {ECO:0000250}.
CC   -!- SUBUNIT: The VTC complex is an integral membrane heterooligomer
CC       composed of at least vtc1, vtc2 and vtc4. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the VTC2/3 family. {ECO:0000305}.
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DR   EMBL; CU329670; CAB11204.1; -; Genomic_DNA.
DR   PIR; T37696; T37696.
DR   RefSeq; NP_594916.1; NM_001020348.2.
DR   AlphaFoldDB; O13718; -.
DR   SMR; O13718; -.
DR   BioGRID; 277933; 15.
DR   STRING; 4896.SPAC14C4.11.1; -.
DR   iPTMnet; O13718; -.
DR   MaxQB; O13718; -.
DR   PaxDb; O13718; -.
DR   PRIDE; O13718; -.
DR   EnsemblFungi; SPAC14C4.11.1; SPAC14C4.11.1:pep; SPAC14C4.11.
DR   GeneID; 2541428; -.
DR   KEGG; spo:SPAC14C4.11; -.
DR   PomBase; SPAC14C4.11; vtc2.
DR   VEuPathDB; FungiDB:SPAC14C4.11; -.
DR   eggNOG; KOG1161; Eukaryota.
DR   eggNOG; KOG4580; Eukaryota.
DR   HOGENOM; CLU_009308_2_0_1; -.
DR   InParanoid; O13718; -.
DR   OMA; SFKFWIH; -.
DR   PhylomeDB; O13718; -.
DR   PRO; PR:O13718; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; ISO:PomBase.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0033254; C:vacuolar transporter chaperone complex; ISO:PomBase.
DR   GO; GO:0006914; P:autophagy; ISO:PomBase.
DR   GO; GO:0006112; P:energy reserve metabolic process; IC:PomBase.
DR   GO; GO:0006799; P:polyphosphate biosynthetic process; ISO:PomBase.
DR   GO; GO:0007034; P:vacuolar transport; ISO:PomBase.
DR   GO; GO:0042144; P:vacuole fusion, non-autophagic; ISO:PomBase.
DR   Gene3D; 3.20.100.30; -; 1.
DR   InterPro; IPR003807; DUF202.
DR   InterPro; IPR004331; SPX_dom.
DR   InterPro; IPR018966; VTC_domain.
DR   InterPro; IPR042267; VTC_sf.
DR   Pfam; PF02656; DUF202; 1.
DR   Pfam; PF09359; VTC; 1.
DR   PROSITE; PS51382; SPX; 1.
PE   1: Evidence at protein level;
KW   Chaperone; Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW   Transmembrane helix; Vacuole.
FT   CHAIN           1..734
FT                   /note="Vacuolar transporter chaperone 2"
FT                   /id="PRO_0000116686"
FT   TOPO_DOM        1..624
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        625..645
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        646..650
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        651..671
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        672..693
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        694..714
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        715..734
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000250"
FT   DOMAIN          1..144
FT                   /note="SPX"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00714"
FT   MOD_RES         181
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         529
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         583
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   734 AA;  85445 MW;  2373306038C7F4EE CRC64;
     MRFSDSIEAG IYEPWRDKYM NYPELKHLLK TEEEAPSWGE NDESKFVSVM DAQLEKVYAF
     HLEILKELNE SVDWVKSKVS ASQEPDGPPI SKEEAIKLLE RLDSCTETVK KLEKYTRLNL
     TGFFKIVKKH DKLYPGYSLR PVFQVRLRAC PLGSVQFNPL LAEIFSLYNT LRDGLSAPSN
     SVQVKPKHEH NVDYNSSMYR RRTFRFWVHP DNVMEVKTYI MRHLPVLYYS GKQGFDKDQN
     GVSGILDPIS TCLYLDNSNF DLYSQNLERS EQAYSLRLHW YGKLTPKTDI IVERMVRQGS
     TLSHSEDRFT IREKKVRELL SGRYDFRKVE DDHSTTASDQ KKKLIEDVEQ LIVDNHLQPV
     LRSVYTRTAF QIPGDDEVRI NLDSDWVMIR EDSLDIERPC RDPEDWHRHD IDDADFPYKH
     LRKGEYSRFP YSVLEIRECV RYDEDEPLWI SELRNSHLIS EIDGFSKYEH GVAILFEKYV
     SLLPMWVFSM DQDIRKDLQE VYSHPEGSAG SRNVYIKRRN QRVLKQNMTP EPSQPSPLVN
     RLKANEMHPV SEEPEDNREV YRNEHGDHFN FRSIPGLLKP STYGSFKHHG KTFVTPPHIK
     KPEIPLRVSG PIKVEAKVWL ANERTFLKWL HVVVLLGSLA LALYNSAGER LGQAFGVVYT
     LLAIFIGFYA WKLHAKRSQM IKSRSPAPMT DYWGPLIVGT ALAISLIVNM SFALKDAVYQ
     NLIEPDRLLV KLFT
 
 
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