ID A0A0R3RQ40_9BILA Unreviewed; 834 AA.
AC A0A0R3RQ40;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 2.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Integrin beta {ECO:0000256|RuleBase:RU000633};
OS Elaeophora elaphi.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Elaeophora.
OX NCBI_TaxID=1147741 {ECO:0000313|Proteomes:UP000050640, ECO:0000313|WBParaSite:EEL_0000376001-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:EEL_0000376001-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251,
CC ECO:0000256|RuleBase:RU000633}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004251, 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A0R3RQ40; -.
DR STRING; 1147741.A0A0R3RQ40; -.
DR WBParaSite; EEL_0000376001-mRNA-1; EEL_0000376001-mRNA-1; EEL_0000376001.
DR Proteomes; UP000050640; 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; 4.10.1240.30; -; 1.
DR Gene3D; 1.20.5.100; Cytochrome c1, transmembrane anchor, C-terminal; 1.
DR Gene3D; 2.10.25.10; Laminin; 4.
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; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR InterPro; IPR013111; EGF_extracell.
DR InterPro; IPR040622; I-EGF_1.
DR InterPro; IPR033760; Integrin_beta_N.
DR InterPro; IPR015812; Integrin_bsu.
DR InterPro; IPR014836; Integrin_bsu_cyt_dom.
DR InterPro; IPR012896; Integrin_bsu_tail.
DR InterPro; IPR036349; Integrin_bsu_tail_dom_sf.
DR InterPro; IPR002369; Integrin_bsu_VWA.
DR InterPro; IPR032695; Integrin_dom_sf.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR10082:SF62; INTEGRIN BETA PAT-3; 1.
DR PANTHER; PTHR10082; INTEGRIN BETA SUBUNIT; 1.
DR Pfam; PF07974; EGF_2; 1.
DR Pfam; PF18372; I-EGF_1; 1.
DR Pfam; PF08725; Integrin_b_cyt; 1.
DR Pfam; PF07965; Integrin_B_tail; 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 SMART; SM01242; Integrin_B_tail; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 2.
DR SUPFAM; SSF69687; Integrin beta tail domain; 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 Cell membrane {ECO:0000256|ARBA:ARBA00022475};
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};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000633};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 759..781
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 58..495
FT /note="Integrin beta subunit VWA"
FT /evidence="ECO:0000259|SMART:SM00187"
FT DOMAIN 675..758
FT /note="Integrin beta subunit tail"
FT /evidence="ECO:0000259|SMART:SM01242"
FT DOMAIN 782..828
FT /note="Integrin beta subunit cytoplasmic"
FT /evidence="ECO:0000259|SMART:SM01241"
FT DISULFID 59..69
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 62..97
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 72..86
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 225..229
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 277..330
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 434..446
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 493..497
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 517..556
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 522..531
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 533..547
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 562..567
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 564..599
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 569..584
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 586..591
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 605..610
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 607..638
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 612..621
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 623..630
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 644..649
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 646..697
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 651..665
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 668..671
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 675..684
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 681..753
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
SQ SEQUENCE 834 AA; 93539 MW; 918DF6473F95EE13 CRC64;
MRDRWLTGLK WYIHVICFST TIFIIAVAQE FSANDVTSEV IESKKDFPCY SLPRENYTCS
ACIQFHDTCA WCSKADFDNE NQHPRCDSLE RLIEHGCPEF EIENPKTTLK TTENVELSNA
GDAASEEEAV QLRPQHMVVN IRPKARIRFQ VTYRQAVDYP VDLYYLMDLS YSMKDDKQKL
SELGDLLAER MKAITKNFRL GFGSFIDKKL MPFVDPRPEK QLSPCPEQCA QPYGFKNQMS
LTMDTARFSK EVEEAEISGN LDAPEGGFDA VLQALTCNVS RFYGFYHRIK NSIGWRERAR
KMIVFSTDAG FHYAGDGRMA GVVVPNDGQC HLDNHGYYTK SLDQDYPSVA LLHQKIKERK
ANLIFAVTEK NKDLYKQLSD ALPDVSSSVG VLADDSRNIV SLIEEEYNKI SQKIIMVDNA
NASQGLRLSY RSRCLDGHTL KETNVCDGIK VGDEVSFEVT LEATHCVKER DFNLKIGPSG
LDETLQVDVH VLCDCDCETD RVIHNSPVCH GKGNLVCGVC ICHGTNVGRH CECDAPGLST
VALDAKCKRT NESAICEGRG VCNCGVCECF ERDNMNEKIS GQFCECDNFN CPRHDRKICA
GHGTCDCGQC TCKPGWTGRA CECPLSLDSC MAANGKVCNG QGECICGRCR CFSDGPGNRY
SGPKCEICPT CPSKCVEHKP CVMCQQWQTG PYNETQCDEC AFTVIPVKEL PVLNDTTECQ
FVDPSDDCTF YFLYYEDQRT DNLTVWVKEE KDCPPPVPVL AIVLGVIAGI VILGLILLLV
WKLLTVLHDR AEFAKFDSER LLAKWDTNEN PIYKQATTTF KNPVYVGNNS MKNK
//
