COTH7_RHIO9
ID COTH7_RHIO9 Reviewed; 596 AA.
AC I1BJN3;
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=Invasin CotH7 {ECO:0000303|PubMed:32487760};
DE AltName: Full=Spore coat protein homolog 7 {ECO:0000303|PubMed:32487760};
DE Flags: Precursor;
GN Name=CotH7 {ECO:0000303|PubMed:32487760};
GN ORFNames=RO3G_01117 {ECO:0000312|EMBL:EIE76413.1};
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, INTERACTION WITH HOST ITGB1, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=32487760; DOI=10.1128/mbio.01087-20;
RA Alqarihi A., Gebremariam T., Gu Y., Swidergall M., Alkhazraji S.,
RA Soliman S.S.M., Bruno V.M., Edwards J.E. Jr., Filler S.G., Uppuluri P.,
RA Ibrahim A.S.;
RT "GRP78 and Integrins Play Different Roles in Host Cell Invasion during
RT Mucormycosis.";
RL MBio 11:e01087-e01087(2020).
CC -!- FUNCTION: Promotes invasion of host epithelial cells by adhering to
CC receptors on the host cell surface to facilitate endocytosis of the
CC pathogen into host cells (PubMed:32487760). Probably binds integrin
CC ITGA3:ITGB1 via ITGB1, on the cell surface of host alveolar epithelial
CC cells (PubMed:32487760). {ECO:0000269|PubMed:32487760}.
CC -!- SUBUNIT: Interacts with host integrin beta-1 ITGB1 on the cell surface
CC of host alveolar epithelial cells. {ECO:0000305|PubMed:32487760}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:32487760};
CC Lipid-anchor, GPI-anchor {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown decreases invasion of
CC human alveolar epithelial cells. {ECO:0000269|PubMed:32487760}.
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DR EMBL; CH476732; EIE76413.1; -; Genomic_DNA.
DR SMR; I1BJN3; -.
DR EnsemblFungi; EIE76413; EIE76413; RO3G_01117.
DR VEuPathDB; FungiDB:RO3G_01117; -.
DR eggNOG; ENOG502TA22; Eukaryota.
DR InParanoid; I1BJN3; -.
DR OMA; AKRNWFK; -.
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 GO; GO:0046789; F:host cell surface receptor binding; IDA:UniProtKB.
DR GO; GO:0044651; P:adhesion of symbiont to host epithelial cell; IDA:UniProtKB.
DR GO; GO:0044409; P:entry into host; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; GPI-anchor; Lipoprotein; Membrane;
KW Reference proteome; Signal; Virulence.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..596
FT /note="Invasin CotH7"
FT /evidence="ECO:0000255"
FT /id="PRO_5003637567"
FT PROPEP 568..596
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000453695"
FT REGION 528..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 567
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 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 288
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"
FT CARBOHYD 544
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 596 AA; 66574 MW; 4FD8160A132DE4D8 CRC64;
MKSLSFISLA CLTAVHAASV TFKVIAPTAE SSVQVNINGQ LTQLKAQDED IPYYTGSAEL
NDGQSYKYVV DGAAETFERI LNGTSTKNEF FNRPITYATN IPELPNILSE GSWTRGETTD
PLWDSNYVPS IFVTGKSDEM EDLITNVTKK TYQAKITFIG PENITTIENC TFGLHKPGRK
HNDAKQTWVW TLPEGQYVAK RSWFKIRHME EDPTQLREKL YADIARKMGT YANEANMVRF
FINKEGMGTF NMLDDVIMYS YINAMFYNGN PPQQLGALYD GASGAAFNAS GDMDSFIPNV
ESPLDQDALM PFSKAFAAVD FSNDDQVKAI SQYFDYDQFL RFMVMEFLTA DWDGYWQEQT
NDGAYIDVSD NNKVYYLAQD FDATFGVNLD QERDFVNTPY TDFPTKFPGG ILINKLLENP
TTKATFETYL KTTVQEIFNN ATLGAYVTAR HNFLAPDLKW DRSIKQRSPG NIFGWTYEQT
YQNLFEGVTA PGKEQGGAEW GLLEWVAAKE KAVRSSLKLS ETATTSTSAT IAAPATSESA
SQDNTSDDTD SASTSSSTLN QAAADTSSAS KSAPTFYCLQ LVLYLSLSFK NLYKYI
