ID A0A093IQ66_FULGA Unreviewed; 754 AA.
AC A0A093IQ66;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Integrin beta {ECO:0000256|RuleBase:RU000633};
DE Flags: Fragment;
GN ORFNames=N327_10689 {ECO:0000313|EMBL:KFW04865.1};
OS Fulmarus glacialis (Northern fulmar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Procellariiformes; Procellariidae;
OC Fulmarus.
OX NCBI_TaxID=30455 {ECO:0000313|EMBL:KFW04865.1, ECO:0000313|Proteomes:UP000053806};
RN [1] {ECO:0000313|EMBL:KFW04865.1, ECO:0000313|Proteomes:UP000053806}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N327 {ECO:0000313|EMBL:KFW04865.1};
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; KK598738; KFW04865.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093IQ66; -.
DR Proteomes; UP000053806; 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:UP000053806};
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 704..726
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..439
FT /note="Integrin beta subunit VWA"
FT /evidence="ECO:0000259|SMART:SM00187"
FT DOMAIN 615..703
FT /note="Integrin beta subunit tail"
FT /evidence="ECO:0000259|SMART:SM01242"
FT DOMAIN 727..754
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..666
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 437..441
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 452..464
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 461..500
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 466..475
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 477..491
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 506..511
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 508..543
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 513..528
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 530..535
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 549..554
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 551..582
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 556..565
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 567..574
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 588..593
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 590..636
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 595..605
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 608..611
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 615..624
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 621..698
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 640..674
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFW04865.1"
FT NON_TER 754
FT /evidence="ECO:0000313|EMBL:KFW04865.1"
SQ SEQUENCE 754 AA; 83297 MW; 8CC9C03F430CA55E CRC64;
CIKANAKSCG ECIQAGPNCG WCKKTDFLQE GEPTSARCDD LAALKSKGCP MEDIENPRGS
KQVLEDREVT NRKIGAAEKL KPEAITQIQP 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
SKLPKGVTIS YKSFCKNGVN DTQEDGRKCS NISIGDEVKF EINVTANECP KKGQNETIKI
KPLGFTEEVE INLQFICECQ CQSEGEPNSP ACHEGNGTFE CGACRCNEGR IGRLCECSTD
EVNSEDMDAY CRRENSTEIC SNNGECICGQ CVCKKRENTN EVYSGKYCEC DNFNCDRSNG
LICGGNGICK CRVCECFPNF TGSACDCSLD TLPCMASNGQ VCNGRGTCEC GTCNCTDPKF
QGPTCEMCQT CLGVCAEHKD CVQCRAFDKG EKKETCSQEC MHFNMTRVES RDKLPQPGQP
DPLSHCKEKD VDDCWFYFTY SVNSNGEANV HVVETPECPS GPDIIPIVAG VVAGIVLIGL
ALLLIWKLLM IIHDRREFAK FEKEKMNAKW DTVS
//
