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IVN1_SCHPO
ID   IVN1_SCHPO              Reviewed;         371 AA.
AC   Q96WW4; O13599;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 105.
DE   RecName: Full=Invasion protein 1;
GN   Name=ivn1; ORFNames=pi004, SPACTOKYO_453.33c, SPBC11B10.07c;
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] {ECO:0000312|EMBL:BAA21381.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=10620777;
RX   DOI=10.1002/(sici)1097-0061(20000115)16:1<71::aid-yea505>3.0.co;2-5;
RA   Machida M., Yamazaki S., Kunihiro S., Tanaka T., Kushida N., Jinno K.,
RA   Haikawa Y., Yamazaki J., Yamamoto S., Sekine M., Oguchi A., Nagai Y.,
RA   Sakai M., Aoki K., Ogura K., Kudoh Y., Kikuchi H., Zhang M.Q., Yanagida M.;
RT   "A 38 kb segment containing the cdc2 gene from the left arm of fission
RT   yeast chromosome II: sequence analysis and characterization of the genomic
RT   DNA and cDNAs encoded on the segment.";
RL   Yeast 16:71-80(2000).
RN   [2] {ECO:0000312|EMBL:CAC37511.1}
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   [3] {ECO:0000305}
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   [4]
RP   FUNCTION.
RX   PubMed=19542312; DOI=10.1128/ec.00078-09;
RA   Dodgson J., Avula H., Hoe K.L., Kim D.U., Park H.O., Hayles J.,
RA   Armstrong J.;
RT   "Functional genomics of adhesion, invasion, and mycelial formation in
RT   Schizosaccharomyces pombe.";
RL   Eukaryot. Cell 8:1298-1306(2009).
CC   -!- FUNCTION: Required for invasive growth. {ECO:0000269|PubMed:19542312}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC       {ECO:0000269|PubMed:16823372}. Membrane {ECO:0000255}; Multi-pass
CC       membrane protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the CDC50/LEM3 family. {ECO:0000255}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA21381.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AB004534; BAA21381.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CU329671; CAC37511.1; -; Genomic_DNA.
DR   RefSeq; NP_595627.1; NM_001021521.2.
DR   AlphaFoldDB; Q96WW4; -.
DR   SMR; Q96WW4; -.
DR   BioGRID; 276281; 35.
DR   STRING; 4896.SPBC11B10.07c.1; -.
DR   MaxQB; Q96WW4; -.
DR   PaxDb; Q96WW4; -.
DR   EnsemblFungi; SPBC11B10.07c.1; SPBC11B10.07c.1:pep; SPBC11B10.07c.
DR   GeneID; 2539729; -.
DR   KEGG; spo:SPBC11B10.07c; -.
DR   PomBase; SPBC11B10.07c; ivn1.
DR   VEuPathDB; FungiDB:SPBC11B10.07c; -.
DR   eggNOG; KOG2952; Eukaryota.
DR   HOGENOM; CLU_025025_0_1_1; -.
DR   InParanoid; Q96WW4; -.
DR   OMA; AWQPMLS; -.
DR   PhylomeDB; Q96WW4; -.
DR   PRO; PR:Q96WW4; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR   GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; ISO:PomBase.
DR   GO; GO:0005770; C:late endosome; ISO:PomBase.
DR   GO; GO:1990531; C:phospholipid-translocating ATPase complex; ISO:PomBase.
DR   GO; GO:0005886; C:plasma membrane; ISO:PomBase.
DR   GO; GO:0045332; P:phospholipid translocation; ISO:PomBase.
DR   InterPro; IPR005045; CDC50/LEM3_fam.
DR   PANTHER; PTHR10926; PTHR10926; 1.
DR   Pfam; PF03381; CDC50; 1.
DR   PIRSF; PIRSF015840; DUF284_TM_euk; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Glycoprotein; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..371
FT                   /note="Invasion protein 1"
FT                   /id="PRO_0000316867"
FT   TRANSMEM        40..60
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        326..346
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        99
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        190
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        212
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        216
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        233
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        284
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        297
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   371 AA;  42421 MW;  E1C2D56A1A72CDE5 CRC64;
     MSQTEIVKKP KHKRFKRPDK SRFVQQTLPA WQFIFTPWTV LPLLFLLGIV FAPLGAGMFV
     ASRRVKELRI DYTDCMNIGD EFKQVPSTNI EFQYKNVKNV TAMWKSSGDV CTLRFQIPEE
     MTSPVFAFYR LKNFYQNHRR YTVSADMFQL LGEARTVAQL KSYGFCKPLE ANEEGKPYYP
     CGIIANSLFN DSYSSLLRYE SFDSSNSLGL YNMTTNGTAW PEDRERYKKT KYNASQIVPP
     PNWAKMFPNG YTDDNIPDVS TWDAFQIWMR AAALPTFSKL ALRNVTTALQ PGIYEMNITY
     NFPVTEYKGT KTIMFSTTSV IGGKNYFLGI LYFVIGGLCA ASGVILSIAC LIKPRRVGDP
     RYLSWNRGKS S
 
 
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