ID A0A0K0JT35_BRUMA Unreviewed; 820 AA.
AC A0A0K0JT35;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Integrin beta {ECO:0000256|RuleBase:RU000633};
GN Name=bma-pat-3 {ECO:0000313|WormBase:Bm7611};
GN Synonyms=Bma-pat-3 {ECO:0000313|EMBL:CDP96636.1,
GN ECO:0000313|WBParaSite:Bm7611.1};
GN ORFNames=Bm7611 {ECO:0000313|WormBase:Bm7611}, BM_Bm7611
GN {ECO:0000313|EMBL:CDP96636.1};
OS Brugia malayi (Filarial nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX NCBI_TaxID=6279 {ECO:0000313|Proteomes:UP000006672, ECO:0000313|WBParaSite:Bm7611.1};
RN [1] {ECO:0000313|EMBL:CDP96636.1, ECO:0000313|Proteomes:UP000006672}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FR3 {ECO:0000313|EMBL:CDP96636.1,
RC ECO:0000313|Proteomes:UP000006672};
RX PubMed=17885136; DOI=10.1126/science.1145406;
RA Ghedin E., Wang S., Spiro D., Caler E., Zhao Q., Crabtree J., Allen J.E.,
RA Delcher A.L., Guiliano D.B., Miranda-Saavedra D., Angiuoli S.V., Creasy T.,
RA Amedeo P., Haas B., El-Sayed N.M., Wortman J.R., Feldblyum T., Tallon L.,
RA Schatz M., Shumway M., Koo H., Salzberg S.L., Schobel S., Pertea M.,
RA Pop M., White O., Barton G.J., Carlow C.K., Crawford M.J., Daub J.,
RA Dimmic M.W., Estes C.F., Foster J.M., Ganatra M., Gregory W.F.,
RA Johnson N.M., Jin J., Komuniecki R., Korf I., Kumar S., Laney S., Li B.W.,
RA Li W., Lindblom T.H., Lustigman S., Ma D., Maina C.V., Martin D.M.,
RA McCarter J.P., McReynolds L., Mitreva M., Nutman T.B., Parkinson J.,
RA Peregrin-Alvarez J.M., Poole C., Ren Q., Saunders L., Sluder A.E.,
RA Smith K., Stanke M., Unnasch T.R., Ware J., Wei A.D., Weil G.,
RA Williams D.J., Zhang Y., Williams S.A., Fraser-Liggett C., Slatko B.,
RA Blaxter M.L., Scott A.L.;
RT "Draft genome of the filarial nematode parasite Brugia malayi.";
RL Science 317:1756-1760(2007).
RN [2] {ECO:0000313|EMBL:CDP96636.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FR3 {ECO:0000313|EMBL:CDP96636.1};
RA Gao Y.W., Fan S.T., Sun H.T., Wang Z., Gao X.L., Li Y.G., Wang T.C.,
RA Zhang K., Xu W.W., Yu Z.J., Xia X.Z.;
RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|WBParaSite:Bm7611.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (DEC-2019) 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}.
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DR EMBL; LN856960; CDP96636.1; -; Genomic_DNA.
DR STRING; 6279.A0A0K0JT35; -.
DR EnsemblMetazoa; Bm7611.1; Bm7611.1; WBGene00227872.
DR WBParaSite; Bm7611.1; Bm7611.1; WBGene00227872.
DR WormBase; Bm7611; BM32508; WBGene00227872; Bma-pat-3.
DR OMA; NCVCGAC; -.
DR OrthoDB; 5475862at2759; -.
DR Proteomes; UP000006672; Unassembled WGS sequence.
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 Reference proteome {ECO:0000313|Proteomes:UP000006672};
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..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..820
FT /note="Integrin beta"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013455930"
FT TRANSMEM 745..767
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 56..481
FT /note="Integrin beta subunit VWA"
FT /evidence="ECO:0000259|SMART:SM00187"
FT DOMAIN 661..744
FT /note="Integrin beta subunit tail"
FT /evidence="ECO:0000259|SMART:SM01242"
FT DOMAIN 768..814
FT /note="Integrin beta subunit cytoplasmic"
FT /evidence="ECO:0000259|SMART:SM01241"
FT DISULFID 57..67
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 60..95
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 70..84
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 223..227
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 275..316
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 420..432
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 479..483
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 503..542
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 508..517
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 519..533
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 548..553
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 550..585
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 555..570
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 572..577
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 591..596
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 593..624
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 598..607
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 609..616
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 630..635
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 632..683
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 637..651
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 654..657
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 661..670
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 667..739
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
SQ SEQUENCE 820 AA; 91839 MW; 749B57C29A200562 CRC64;
MRDRWLTRLG WCRMICLSTT IFIVGAQEFT TDDATSEIVE SKKDFPCYSL PRENYTCSAC
IQFHDTCAWC SKADFDNENQ HPRCDSLERL IEHGCPEFEI ENPKTTVRTT ENVELSNAGD
AASEEEAVQL RPQHMVVNIR PKARVRFQVT YRQAVDYPVD LYYLMDLSYS MKDDKQKLSE
LGDLLAERMK AITKNFRLGF GSFIDKKLMP FVDPRPEKQL SPCPEQCAQP YGFKNQMSLT
MDTNRFSKEV EEAEISGNLD APEGGFDAVL QALTCNNSIG WRERARKMIV FSTDAGFHYA
GDGRMAGVVV PNDGQCHLDS QGYYTKSLDQ DYPSVALLHQ KIKERKANLI FAVTEKNKDL
YKQLSDALPD VSSSVGVLAD DSRNIVSLIE EEYNKISQKI IMVDNANASQ GLRLSYRSRC
LDGHTLKETN VCDGIKVGDE VSFEVTLEAT HCVKERDFNL KIGPSGLDET LQVDVHVQCD
CDCETDRVVY NSPICHGKGD LVCGVCICHG TNVGRHCECD APGLSTVALD AKCKRTNESA
ICEGRGVCNC GVCECFERDN MNEKISGQFC ECDNFNCPRH DRKICAGHGT CDCGQCTCKP
GWTGRACECP LSLDSCMAAN GKVCNGQGEC ICGRCRCFSD GPGNRYSGPK CEICPTCPSK
CVEHKPCVMC QQWQTGPYNE TQCDECTFTV IPVKELPVLN DTTECQFVDP SDDCTFYFLY
YEDQRTDNLT VWVKEEKDCP PPVPVLAIVL GVIAGIVILG LILLLVWKLL TVLHDRAEFA
KFDSERLLAK WDTNENPIYK QATTTFKNPV YVGNNTMKNK
//
