ID A0A093NS85_PYGAD Unreviewed; 764 AA.
AC A0A093NS85;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Integrin beta {ECO:0000256|RuleBase:RU000633};
DE Flags: Fragment;
GN ORFNames=AS28_12856 {ECO:0000313|EMBL:KFW64845.1};
OS Pygoscelis adeliae (Adelie penguin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae; Pygoscelis.
OX NCBI_TaxID=9238 {ECO:0000313|EMBL:KFW64845.1, ECO:0000313|Proteomes:UP000054081};
RN [1] {ECO:0000313|EMBL:KFW64845.1, ECO:0000313|Proteomes:UP000054081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_AS28 {ECO:0000313|EMBL:KFW64845.1};
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}.
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 EMBL; KL224844; KFW64845.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093NS85; -.
DR STRING; 9238.A0A093NS85; -.
DR Proteomes; UP000054081; 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; 2.
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; 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:SF15; INTEGRIN BETA-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.
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:UP000054081};
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..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..764
FT /note="Integrin beta"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001886423"
FT TRANSMEM 697..722
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 26..69
FT /note="PSI"
FT /evidence="ECO:0000259|SMART:SM00423"
FT DOMAIN 34..443
FT /note="Integrin beta subunit VWA"
FT /evidence="ECO:0000259|SMART:SM00187"
FT DOMAIN 617..696
FT /note="Integrin beta subunit tail"
FT /evidence="ECO:0000259|SMART:SM01242"
FT DOMAIN 720..764
FT /note="Integrin beta subunit cytoplasmic"
FT /evidence="ECO:0000259|SMART:SM01241"
FT DISULFID 27..443
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 35..45
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 38..68
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 48..57
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 187..194
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 242..282
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 416..658
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 441..445
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 462..501
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 467..476
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 478..492
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 507..512
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 509..544
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 514..529
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 531..536
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..638
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 598..607
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 610..613
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 617..626
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 623..691
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 642..666
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT NON_TER 764
FT /evidence="ECO:0000313|EMBL:KFW64845.1"
SQ SEQUENCE 764 AA; 84733 MW; B424F4EBBB3B4D67 CRC64;
MSRDCRLQLP AVTWVLLLVM TAFAMECPKI KVGTCKDCIQ SGPGCAWCKK PVDSIRCDTI
EQLQQRGCPH NEIEFPGNDI TKTQNSPLSN DTQLTPQEVH LKLRIGQPAV FEVKFRRAMG
YPIDLYYLMD LSYSMLDDLE KVKKLGGELL RALESTTPSR RIGFGSFVDK TVLPFVNTHP
EKLQNPCPNK DKECQPPFAF KHILSLTDNA KKFESEVGKQ FISGNLDAPE GGLDAMMQAA
VCGDLIGWRN VTRLLVYATD DGFHFAGDGK LGAILTPNDG QCHLEDNMYK KSNEFDYPSV
GQLVQKLAEN NIQPIFAVTS KMVDVYKKLS EMIPKSAVGE LNEDSSNIIE LIQVAYNNLS
SRIILDHSTL PDVLDVKYDS ICSKDKVILD EARGQCDNVK INDEVIFKVK VTAKECIKSQ
SFTIRPLGFT DTLTVHLDSN CNCNCNEQPD PTACSGKGSI ICGICSCNSG YTGKNCECET
KGKTSKELEG SCRKDNSSVI CSGLGDCVCG QCICHTSDVP DKQIYGTFCE CDNMNCEFHN
GSLCGGKDRG RCDCGECKCL PEYQGSACQC KKSTDGCLNI RGNECSHRGT CHCNRCQCRG
GYQPPFCQEC PGCPSPCGRY VSCVECKAFL SGPFEKNCSQ VCSNIQVTEK LTGVSRQCRE
KDSHNCWISF RMVQEDGEEM YSVIVDRKKE CPEPPNIALI VGGTIAGVAL IGLVLLLIWR
LLTELFDRRE YRRFEKEKSK AKWNDADNPL FKSATTTVVN PRFN
//