ID   INVA_YEREN              Reviewed;         835 AA.
AC   P19196;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Invasin;
OS   Yersinia enterocolitica.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=630;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=8081C / Serotype O:8;
RX   PubMed=2233250; DOI=10.1111/j.1365-2958.1990.tb00686.x;
RA   Young V.B., Miller V.L., Falkow S., Schoolnik G.K.;
RT   "Sequence, localization and function of the invasin protein of Yersinia
RT   enterocolitica.";
RL   Mol. Microbiol. 4:1119-1128(1990).
CC   -!- FUNCTION: Invasin is a protein that allows enteric bacteria to
CC       penetrate cultured mammalian cells. The entry of invasin in the cell is
CC       mediated by binding several beta-1 chain integrins.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane.
CC   -!- SIMILARITY: Belongs to the intimin/invasin family. {ECO:0000305}.
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DR   EMBL; X53368; CAA37448.1; -; Genomic_DNA.
DR   PIR; S11442; S11442.
DR   AlphaFoldDB; P19196; -.
DR   SMR; P19196; -.
DR   GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   Gene3D; 2.40.160.160; -; 1.
DR   Gene3D; 2.60.40.10; -; 2.
DR   Gene3D; 3.10.100.10; -; 1.
DR   InterPro; IPR003344; Big_1_dom.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR016187; CTDL_fold.
DR   InterPro; IPR024519; IAT_beta.
DR   InterPro; IPR038177; IAT_beta_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003535; Intimin/invasin_bac.
DR   InterPro; IPR013117; Intimin_C.
DR   InterPro; IPR008964; Invasin/intimin_cell_adhesion.
DR   InterPro; IPR015217; Invasin_dom_3.
DR   Pfam; PF02369; Big_1; 1.
DR   Pfam; PF11924; IAT_beta; 1.
DR   Pfam; PF07979; Intimin_C; 1.
DR   Pfam; PF09134; Invasin_D3; 1.
DR   PRINTS; PR01369; INTIMIN.
DR   SMART; SM00634; BID_1; 1.
DR   SUPFAM; SSF49373; SSF49373; 3.
DR   SUPFAM; SSF56436; SSF56436; 1.
DR   PROSITE; PS51127; BIG1; 1.
PE   3: Inferred from homology;
KW   Cell outer membrane; Membrane.
FT   CHAIN           1..835
FT                   /note="Invasin"
FT                   /id="PRO_0000211830"
FT   DOMAIN          451..541
FT                   /note="Big-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00445"
SQ   SEQUENCE   835 AA;  91361 MW;  6133FF9FDB8D9BBA CRC64;
     MYSFFNTLTV TKIISRLILS IGLIFGIFTY GFSQQHYFNS EALENPAEHN EAFNKIISTG
     TSLAVSGNAS NITRSMVNDA ANQEVKHWLN RFGTTQVNVN FDKKFSLKES SLDWLLPWYD
     SASYVFFSQL GIRNKDSRNT LNIGAGVRTF QQSWMYGFNT SYDNDMTGHN HRIGVGAEAW
     TDYLQLSANG YFRLNGWHQS RDFADYNERP ASGGDIHVKA YLPALPQLGG KLKYEQYRGE
     RVALFGKDNL QSNPYAVTTG LIYTPIPFIT LGVDQRMGKS RQHEIQWNLQ MDYRLGESFR
     SQFSPAVVAG TRLLAESRYN LVERNPNIVL EYQKQNTIKL AFSPAVLSGL PGQVYSVSAQ
     IQSQSALQRI LWNDAQWVAA GGKLIPVSAT DYNVVLPPYK PMAPASRTVG KTGESEAAVN
     TYTLSATAID NHGNSSNPAT LTVIVQQPQF VITSEVTDDG ALADGRTPIT VKFTVTNIDS
     TPVAEQEGVI TTSNGALPSK VTKKTDAQGV ISIALTSFTV GVSVVTLDIQ GQQATVDVRF
     AVLPPDVTNS SFNVSPSDIV ADGSMQSILT FVPRNKNNEF VSGITDLEFI QSGVPVTISP
     VTENADNYTA SVVGNSVGDV DITPQVGGES LDLLQKRITL YPVPKITGIN VNGEQFATDK
     GFPKTTFNKA TFQLVMNDDV ANNTQYDWTS SYAASAPVDN QGKVNIAYKT YGSTVTVTAK
     SKKFPSYTAT YQFKPNLWVF SGTMSLQSSV EASRNCQRTD FTALIESARA SNGSRSPDGT
     LWGEWGSLAT YDSAEWPSGN YWTKKTSTDF VTMDMTTGDI PTSAATAYPL CAEPQ