ID A0A016VF04_9BILA Unreviewed; 830 AA.
AC A0A016VF04;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Integrin beta {ECO:0000256|RuleBase:RU000633};
GN Name=Acey_s0011.g1500 {ECO:0000313|EMBL:EYC25995.1};
GN Synonyms=Acey-pat-3 {ECO:0000313|EMBL:EYC25995.1};
GN ORFNames=Y032_0011g1500 {ECO:0000313|EMBL:EYC25995.1};
OS Ancylostoma ceylanicum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=53326 {ECO:0000313|EMBL:EYC25995.1, ECO:0000313|Proteomes:UP000024635};
RN [1] {ECO:0000313|Proteomes:UP000024635}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX PubMed=25730766; DOI=10.1038/ng.3237;
RA Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA Aroian R.V.;
RT "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT ceylanicum identify infection-specific gene families.";
RL Nat. Genet. 47:416-422(2015).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EYC25995.1}.
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DR EMBL; JARK01001347; EYC25995.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A016VF04; -.
DR STRING; 53326.A0A016VF04; -.
DR Proteomes; UP000024635; 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; 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; 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:UP000024635};
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..34
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 35..830
FT /note="Integrin beta"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001489346"
FT TRANSMEM 756..778
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 67..492
FT /note="Integrin beta subunit VWA"
FT /evidence="ECO:0000259|SMART:SM00187"
FT DOMAIN 672..755
FT /note="Integrin beta subunit tail"
FT /evidence="ECO:0000259|SMART:SM01242"
FT DOMAIN 779..825
FT /note="Integrin beta subunit cytoplasmic"
FT /evidence="ECO:0000259|SMART:SM01241"
FT DISULFID 68..78
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 71..106
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 81..95
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 234..238
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 286..327
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 431..443
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 490..494
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 514..553
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 519..528
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 530..544
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 559..564
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 561..596
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 566..581
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 583..588
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 602..607
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 604..635
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 609..618
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 620..627
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 641..646
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 643..694
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 648..662
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 665..668
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 672..681
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 678..750
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
SQ SEQUENCE 830 AA; 92610 MW; 128B9C20993D654A CRC64;
MAGSVVFERN TAAGQLTEML GHVIPLLLVS ATLAAEVSDW KTGDVTGEVV EGRKDFPCYS
LSRDNYTCSA CIQLHDSCAW CGAPLFDAKK QYARCDNRAR LLEHGCPESY IEDPQTILEV
EKDEPLSDKG QVENEDDAVQ LKPQEMFVEI RPKSRVRFNV TYRQAVDYPV DLYYLMDLSY
SMKDDKQKLS ELGDLLAVRM RNITKNFRLG FGSFIDKKLM PFIDPRIEKQ KSPCAEPCAE
PYGFKHQMTL TTNTEKFKAE VDKAEISGNL DAPEGGFDAV VQALACNSKI GWRERARKMV
VFSTDAGFHF AGDGRLAGVV EPNDGECHLD RDGYYTETLN QDYPSIALLH QMIKDRKANI
IFAVTKGNHE LYTQLSESLP DVSSSVGILE TDSRNIVDLI EGEYLKISEK IIMVDNANAS
DGLKITYRSM CLDGTTLRDT NVCEGIRVGD EVQFEVTLEA THCVEKRDFV LRIGPSGLDE
TLIVNVKVLC DCDCEQEDRI VENAEECHGG DMVCGVCRCK GGNVGRYCEC NRPGMSTAAL
NEKCKRTNES AICEGRGVCN CGRCECNPRQ NPEEQISGEF CECDNFNCPR HDRKICAEHG
ECNCGQCICA PGWTGRACEC PISQDSCMSA NGKICNGKGE CICGRCRCFD GPDGNRYSGA
KCEICPTCPT KCIEYKPCVM CQQWGTGPYD EERCAECPFK VIPVEELPEL NETTACQFVD
PADDCTFYYL YYYDEATDNA TVWVREHKDC PPPVPVLAIV LGVIAGIVIL GLILLLVWKL
LTVLHDRAEY AKFNNERLMA KWDTNENPIY KQATTTFRNP VYAGNKNKGL
//
