ID A0A1I8GB32_9PLAT Unreviewed; 812 AA.
AC A0A1I8GB32;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Integrin beta {ECO:0000256|RuleBase:RU000633};
OS Macrostomum lignano.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX NCBI_TaxID=282301 {ECO:0000313|Proteomes:UP000095280, ECO:0000313|WBParaSite:maker-uti_cns_0001402-snap-gene-0.5-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:maker-uti_cns_0001402-snap-gene-0.5-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU000633};
CC Single-pass type I membrane protein {ECO:0000256|RuleBase:RU000633}.
CC Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane
CC protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the integrin beta chain family.
CC {ECO:0000256|ARBA:ARBA00007449, ECO:0000256|RuleBase:RU000633}.
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DR AlphaFoldDB; A0A1I8GB32; -.
DR WBParaSite; maker-uti_cns_0001402-snap-gene-0.5-mRNA-1; maker-uti_cns_0001402-snap-gene-0.5-mRNA-1; maker-uti_cns_0001402-snap-gene-0.5.
DR Proteomes; UP000095280; Unplaced.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 1.20.5.100; Cytochrome c1, transmembrane anchor, C-terminal; 1.
DR Gene3D; 2.10.25.10; Laminin; 1.
DR Gene3D; 3.30.1680.10; ligand-binding face of the semaphorins, domain 2; 1.
DR Gene3D; 2.60.40.1510; ntegrin, alpha v. Chain A, domain 3; 1.
DR Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 1.
DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR InterPro; IPR033760; Integrin_beta_N.
DR InterPro; IPR015812; Integrin_bsu.
DR InterPro; IPR014836; Integrin_bsu_cyt_dom.
DR InterPro; IPR002369; Integrin_bsu_VWA.
DR InterPro; IPR032695; Integrin_dom_sf.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR10082; INTEGRIN BETA SUBUNIT; 1.
DR PANTHER; PTHR10082:SF60; INTEGRIN BETA-PS; 1.
DR Pfam; PF08725; Integrin_b_cyt; 1.
DR Pfam; PF00362; Integrin_beta; 1.
DR Pfam; PF17205; PSI_integrin; 1.
DR PIRSF; PIRSF002512; Integrin_B; 1.
DR PRINTS; PR01186; INTEGRINB.
DR SMART; SM00187; INB; 1.
DR SMART; SM01241; Integrin_b_cyt; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF69179; Integrin domains; 1.
DR SUPFAM; SSF103575; Plexin repeat; 1.
DR SUPFAM; SSF53300; vWA-like; 1.
DR PROSITE; PS00243; INTEGRIN_BETA; 1.
PE 3: Inferred from homology;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889,
KW ECO:0000256|RuleBase:RU000633};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR002512-1};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Integrin {ECO:0000256|ARBA:ARBA00023037, ECO:0000256|RuleBase:RU000633};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000633};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..812
FT /note="Integrin beta"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009319256"
FT TRANSMEM 749..770
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 43..469
FT /note="Integrin beta subunit VWA"
FT /evidence="ECO:0000259|SMART:SM00187"
FT DOMAIN 771..812
FT /note="Integrin beta subunit cytoplasmic"
FT /evidence="ECO:0000259|SMART:SM01241"
FT DISULFID 44..54
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 47..84
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 57..73
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 199..208
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 256..298
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 408..420
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 467..472
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 493..529
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 498..507
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 535..540
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 537..569
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 542..552
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 577..583
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 585..594
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 596..606
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 624..629
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 631..641
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 652..663
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 660..742
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
SQ SEQUENCE 812 AA; 89580 MW; 15CE185BCA958DFB CRC64;
KLFQLLKTIM LLPKSLFLAL LCSATVTIVS SISPCSVGIP PTSCSACIKL HSSCAWCTDE
SFDDSRIGPQ HRCGTKAELR DRGCILMESP VSRAEIMLDN PLSDSNQIKP QNVSVWARTH
HSIQLEFEFK QAENYPVDMY ILSDKSHSMR DFLQSVANMS EKIQQTLGEL TRNWRIGVGF
FVDKPVFPYV QPNPSAAPCD SLGFGERCID TFSYIHAMDL SQNVAELKEV TAAKTISANL
DAPEGSLDAL LQAVICRSQI GWRSNSRKVV LLAIDGGFHM AGDGRFGGII EPFPESQCHL
ETGRNKLNVT GSLEYVNATR FDYPSIGQVA KVLSDAKVSV IFALKSDSYT PLYMQLKHAL
PVVTEVDLVT NDNVLELIKK NYRSIAETVE IRANDPGLWL NITSEVRCPG ETDFKLGNRC
HRVPLGATVS YRATVTLTKC LPRPEEIVHF ASTTSDDRME VRIKSLCNCP ECEAKANPLQ
KVPKCQNVGH LECGVCSCHG NYSGDSCQCD AQTGSQVDQC HSGDVSNICS KNGRCVCNKC
VCYKDNYYGK LCELDKLSCP DSWDTKEPCG GPSRGECDGK RTCICKPGYS EKDCSCSDAN
KLKPDCHSKK EQYKDMQCSN HGTCICGRCV CEALWSSDPH CDTKAGSTGS LCNDEGLRRC
VECVFNHRKL APEDRQTQCN CSLVEEGVWI DASNEVINDK STCVLNMANE CSLLYGYIIG
DGSIGSRSIR NMTLFIQEEK QCRDRVSPLI LVLIVVAAVV IVGIIILLIW KALITISDRR
EFAKFKSQTQ NSAWGAGENP VYRDPNTTVT NP
//
