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CFR1_SCHPO
ID   CFR1_SCHPO              Reviewed;         620 AA.
AC   Q92357;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=Cell fusion protein cfr1;
DE   AltName: Full=CHS5-related protein 1;
GN   Name=cfr1; ORFNames=SPAC6G9.12;
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   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=16598689; DOI=10.1002/yea.1361;
RA   Cartagena-Lirola H., Duran A., Valdivieso M.-H.;
RT   "The Schizosaccharomyces pombe cfr1(+) gene participates in mating through
RT   a new pathway that is independent of fus1(+).";
RL   Yeast 23:375-388(2006).
CC   -!- FUNCTION: Required for cell fusion, independently of fus1. Appears to
CC       have a role in transporting proteins that are involved in mating. May
CC       act as a scaffold to retain cell fusion proteins in the cisternae of
CC       the Golgi. Degraded at the onset of mating and this leads to release of
CC       cell fusion proteins. {ECO:0000269|PubMed:16598689}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:16598689}.
CC   -!- SIMILARITY: Belongs to the CHS5 family. {ECO:0000305}.
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DR   EMBL; CU329670; CAB03614.1; -; Genomic_DNA.
DR   PIR; T39074; T39074.
DR   RefSeq; NP_594121.1; NM_001019545.2.
DR   AlphaFoldDB; Q92357; -.
DR   SMR; Q92357; -.
DR   BioGRID; 278463; 17.
DR   STRING; 4896.SPAC6G9.12.1; -.
DR   iPTMnet; Q92357; -.
DR   MaxQB; Q92357; -.
DR   PaxDb; Q92357; -.
DR   PRIDE; Q92357; -.
DR   EnsemblFungi; SPAC6G9.12.1; SPAC6G9.12.1:pep; SPAC6G9.12.
DR   GeneID; 2541978; -.
DR   KEGG; spo:SPAC6G9.12; -.
DR   PomBase; SPAC6G9.12; cfr1.
DR   VEuPathDB; FungiDB:SPAC6G9.12; -.
DR   eggNOG; ENOG502QRF7; Eukaryota.
DR   HOGENOM; CLU_019904_3_0_1; -.
DR   InParanoid; Q92357; -.
DR   OMA; TPYEFQL; -.
DR   PhylomeDB; Q92357; -.
DR   PRO; PR:Q92357; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005769; C:early endosome; IDA:PomBase.
DR   GO; GO:0034044; C:exomer complex; IDA:PomBase.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:PomBase.
DR   GO; GO:0005802; C:trans-Golgi network; IDA:PomBase.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0000747; P:conjugation with cellular fusion; IBA:GO_Central.
DR   GO; GO:0006895; P:Golgi to endosome transport; IMP:PomBase.
DR   GO; GO:0006893; P:Golgi to plasma membrane transport; ISO:PomBase.
DR   GO; GO:0006896; P:Golgi to vacuole transport; IPI:PomBase.
DR   CDD; cd13945; Chs5_N; 1.
DR   CDD; cd00063; FN3; 1.
DR   Gene3D; 2.60.40.10; -; 1.
DR   Gene3D; 3.40.50.10190; -; 1.
DR   InterPro; IPR001357; BRCT_dom.
DR   InterPro; IPR036420; BRCT_dom_sf.
DR   InterPro; IPR031673; Chs5_N.
DR   InterPro; IPR031669; Fn3_2.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   Pfam; PF16892; CHS5_N; 1.
DR   Pfam; PF16893; fn3_2; 1.
DR   Pfam; PF12738; PTCB-BRCT; 1.
DR   SMART; SM00292; BRCT; 1.
DR   SMART; SM00060; FN3; 1.
DR   SUPFAM; SSF49265; SSF49265; 1.
DR   SUPFAM; SSF52113; SSF52113; 1.
DR   PROSITE; PS50172; BRCT; 1.
DR   PROSITE; PS50853; FN3; 1.
PE   3: Inferred from homology;
KW   Golgi apparatus; Reference proteome.
FT   CHAIN           1..620
FT                   /note="Cell fusion protein cfr1"
FT                   /id="PRO_0000089660"
FT   DOMAIN          79..169
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          167..256
FT                   /note="BRCT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT   REGION          287..566
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          588..620
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        287..328
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        336..371
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        372..392
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        393..431
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        447..470
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        492..516
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        522..540
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   620 AA;  67230 MW;  7782DD773F5577DA CRC64;
     MDDTNQFMVS VAKIDAGMAI LLTPSFHIIE FPSVLLPNDA TAGSIIDISV HHNKEEEIAR
     ETAFDDVQKE IFETYGQKLP SPPVLKLKNA TQTSIVLEWD PLQLSTARLK SLCLYRNNVR
     VLNISNPMTT HNAKLSGLSL DTEYDFSLVL DTTAGTFPSK HITIKTLRMI DLTGIQVCVG
     NMVPNEMEAL QKCIERIHAR PIQTSVRIDT THFICSSTGG PEYEKAKAAN IPILGLDYLL
     KCESEGRLVN VSGFYIENRA SYNANASINS VEAAQNAAPN LNATTEQPKN TAEVAQGAAS
     AKAPQQTTQQ GTQNSANAEP SSSASVPAEA PETEAEQSID VSSDIGLRSD SSKPNEAPTS
     SENIKADQPE NSTKQENPEE DMQIKDAEEH SNLESTPAAQ QTSEVEANNH QEKPSSLPAV
     EQINVNEENN TPETEGLEDE KEENNTAAES LINQEETTSG EAVTKSTVES SANEEEAEPN
     EIIEENAVKS LLNQEGPATN EEVEKNNANS ENANGLTDEK IIEAPLDTKE NSDDDKPSPA
     AAEDIGTNGA IEEIPQVSEV LEPEKAHTTN LQLNALDKEE DLNITTVKQS SEPTADDNLI
     PNKEAEIIQS SDEFESVNID
 
 
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