ID A0A093G688_DRYPU Unreviewed; 757 AA.
AC A0A093G688;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Integrin beta {ECO:0000256|RuleBase:RU000633};
DE Flags: Fragment;
GN ORFNames=N307_00574 {ECO:0000313|EMBL:KFV64638.1};
OS Dryobates pubescens (Downy woodpecker) (Picoides pubescens).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Piciformes; Picidae; Dryobates.
OX NCBI_TaxID=118200 {ECO:0000313|EMBL:KFV64638.1, ECO:0000313|Proteomes:UP000053875};
RN [1] {ECO:0000313|EMBL:KFV64638.1, ECO:0000313|Proteomes:UP000053875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N307 {ECO:0000313|EMBL:KFV64638.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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}. Cell
CC projection, invadopodium membrane {ECO:0000256|ARBA:ARBA00004297};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004297}.
CC Cell projection, lamellipodium {ECO:0000256|ARBA:ARBA00004510}. Cell
CC projection, ruffle membrane {ECO:0000256|ARBA:ARBA00004199}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004199}.
CC Melanosome {ECO:0000256|ARBA:ARBA00004223}. Membrane
CC {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC {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; KL215443; KFV64638.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093G688; -.
DR STRING; 118200.A0A093G688; -.
DR Proteomes; UP000053875; Unassembled WGS sequence.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0032587; C:ruffle 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 GO; GO:0007517; P:muscle organ development; 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; IPR016201; PSI.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR10082; INTEGRIN BETA SUBUNIT; 1.
DR PANTHER; PTHR10082:SF28; INTEGRIN BETA-1; 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 SMART; SM00423; PSI; 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 junction {ECO:0000256|ARBA:ARBA00022949};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
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 Myogenesis {ECO:0000256|ARBA:ARBA00022541};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000053875};
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 707..729
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..50
FT /note="PSI"
FT /evidence="ECO:0000259|SMART:SM00423"
FT DOMAIN 8..442
FT /note="Integrin beta subunit VWA"
FT /evidence="ECO:0000259|SMART:SM00187"
FT DOMAIN 618..706
FT /note="Integrin beta subunit tail"
FT /evidence="ECO:0000259|SMART:SM01242"
FT DOMAIN 730..757
FT /note="Integrin beta subunit cytoplasmic"
FT /evidence="ECO:0000259|SMART:SM01241"
FT DISULFID 9..19
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 12..49
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 22..38
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 181..187
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 235..275
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 409..669
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 440..444
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 455..467
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 464..503
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 469..478
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 480..494
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 509..514
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 511..546
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 516..531
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 533..538
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 552..557
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 554..585
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 559..568
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 570..577
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 591..596
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 593..639
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 598..608
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 611..614
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 618..627
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 624..701
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 643..677
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFV64638.1"
FT NON_TER 757
FT /evidence="ECO:0000313|EMBL:KFV64638.1"
SQ SEQUENCE 757 AA; 83755 MW; 5C9941E7D65AA0BF CRC64;
CIKANAKHCG ECIQAGPNCG WCKKPDFLQE GEPTSARCDD LAALKSKGCP LEDIENPRGS
KQVLEDREVT NRKIGAAEKL DPQDITQIQP QKLVLKLRVG EPQTFSLKFK RAEDYPIDLY
YLMDLSYSMK DDLENVKSLG TALMLEMEKI TSDFRIGFGS FVEKTVMPYI STTPAKLRNP
CTGDQNCTSP FSYKNVLSLT SEGNKFNELV GKQHISGNLD SPEGGFDAIM QVAVCGEQIG
WRNVTRLLVF STDAGFHFAG DGKLGGIVLP NDGKCHLENN MYTMSHYYDY PSIAHLVQKL
SENNIQTIFA VTEEFQAVYK ELKNLIPKSA VGTLSSNSSN VIQLIIDAYN SLSSEVILEN
TKLPKGVTIS YKSFCKNGVN DTQEDGRKCS NISIGDEVKF EINVTANECP QKGQNETTTT
IRIKPLGFTE EVEINLQFIC ECQCQGEGEP NSPICHEGNG TFECGACRCN EGRIGRLCEC
STDEVNSEDM DAYCRRENST EICSNNGECI CGQCVCKKRE NTNEVYSGKY CECDNFNCDR
SNGLICGGNG VCKCRVCECY PNFTGSACDC SLDTTPCMAS NGQICNGRGT CECGTCNCTD
PKFQGPTCEM CQTCLGVCAE HKDCVQCRAF DKGEKKESCS QECMYFNMTR VENRDKLPQP
GQPDPLSHCK EKDVDDCWFY FTYSVNSNGE ANVHVVETPE CPSGPDIIPI VAGVVAGIVL
IGLALLLIWK LLMIIHDRRE FAKFEKEKMN AKWDTVS
//
