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COTH1_RHIO9
ID   COTH1_RHIO9             Reviewed;         609 AA.
AC   I1BVT3;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2012, sequence version 1.
DT   25-MAY-2022, entry version 31.
DE   RecName: Full=Spore coat protein homolog 1 {ECO:0000303|PubMed:24355926};
DE   Flags: Precursor;
GN   Name=CotH1 {ECO:0000303|PubMed:24355926};
GN   ORFNames=RO3G_05018 {ECO:0000312|EMBL:EIE80313.1};
OS   Rhizopus delemar (strain RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL
OS   43880) (Mucormycosis agent) (Rhizopus arrhizus var. delemar).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX   NCBI_TaxID=246409 {ECO:0000312|Proteomes:UP000009138};
RN   [1] {ECO:0000312|Proteomes:UP000009138}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL 43880
RC   {ECO:0000312|Proteomes:UP000009138};
RX   PubMed=19578406; DOI=10.1371/journal.pgen.1000549;
RA   Ma L.-J., Ibrahim A.S., Skory C., Grabherr M.G., Burger G., Butler M.,
RA   Elias M., Idnurm A., Lang B.F., Sone T., Abe A., Calvo S.E.,
RA   Corrochano L.M., Engels R., Fu J., Hansberg W., Kim J.-M., Kodira C.D.,
RA   Koehrsen M.J., Liu B., Miranda-Saavedra D., O'Leary S.,
RA   Ortiz-Castellanos L., Poulter R., Rodriguez-Romero J., Ruiz-Herrera J.,
RA   Shen Y.-Q., Zeng Q., Galagan J., Birren B.W., Cuomo C.A., Wickes B.L.;
RT   "Genomic analysis of the basal lineage fungus Rhizopus oryzae reveals a
RT   whole-genome duplication.";
RL   PLoS Genet. 5:E1000549-E1000549(2009).
RN   [2] {ECO:0000305}
RP   FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX   PubMed=24355926; DOI=10.1172/jci71349;
RA   Gebremariam T., Liu M., Luo G., Bruno V., Phan Q.T., Waring A.J.,
RA   Edwards J.E. Jr., Filler S.G., Yeaman M.R., Ibrahim A.S.;
RT   "CotH3 mediates fungal invasion of host cells during mucormycosis.";
RL   J. Clin. Invest. 124:237-250(2014).
CC   -!- FUNCTION: May play a role in cell adhesion.
CC       {ECO:0000305|PubMed:24355926}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24355926};
CC       Lipid-anchor, GPI-anchor {ECO:0000255}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in spores.
CC       {ECO:0000269|PubMed:24355926}.
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DR   EMBL; CH476734; EIE80313.1; -; Genomic_DNA.
DR   SMR; I1BVT3; -.
DR   EnsemblFungi; EIE80313; EIE80313; RO3G_05018.
DR   VEuPathDB; FungiDB:RO3G_05018; -.
DR   eggNOG; ENOG502TA22; Eukaryota.
DR   InParanoid; I1BVT3; -.
DR   OMA; PVTYANI; -.
DR   OrthoDB; 405193at2759; -.
DR   Proteomes; UP000009138; Unassembled WGS sequence.
DR   GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   Gene3D; 2.60.40.10; -; 1.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014867; Spore_coat_CotH_CotH2/3/7.
DR   Pfam; PF08757; CotH; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Glycoprotein; GPI-anchor; Lipoprotein; Membrane;
KW   Reference proteome; Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..609
FT                   /note="Spore coat protein homolog 1"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5003638187"
FT   PROPEP          585..609
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000453692"
FT   REGION          527..547
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        533..547
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           584
FT                   /note="GPI-anchor amidated serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        82
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        397
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        440
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   609 AA;  68759 MW;  1F53F9B636D32E38 CRC64;
     MKSLLFVVFI FLTTTYAAKV SFKVIAPDAK NRVHVNINGV LVELKASDPD VPYYTGFAEL
     KHGQSYNYVV DGNAEPFKRL LNGSSTKNEF FNRPVTYATN IPELPSILTE GSWTRGDTSN
     PIWDSNYVPS IFVTGNPREM NELIENVKKN TYKTKITFIG PETINTFEGC TLGLHKPGRK
     HNDAKQSWIW ALPEGQFMAN RNWFKIRHME EDPTQLREKL YADILRKMGT YANEANMVRF
     FINKEGMGIF NMLDDVIMYS YINAMFYHGD TPEQLGGLYD GASGASFNFP GDFDSFIPNV
     ESPLDQDAIE PFSKAFTSID FLEDEQVKTI GKYFDYDQFL RFMVMEFLTG DWDGYWQEQT
     NDGAYIDIND HNKIYYLGQD FDATFGVNLE QKREFVNVSY TEYPKLFPGG VLINRLLQNP
     GVKKTFENYL KITVQEIFNN ATLGPYVTAR HEFLAPDLQW DRSIKQRSPG NIFGWTFEQT
     YENLFEGVTA PGKNSGGADW GLLEWVAAKE KAVKSYLSSS EAADAATVTQ VPEAPGTDGT
     PSESTAWPHA NTRFRQAEAS NTHKIGTSSP SNFIVKIKQG TVSSSSSIKR TPCILPLVIL
     ASTLFASFF
 
 
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