ID A0A3B4WK93_SERLL Unreviewed; 799 AA.
AC A0A3B4WK93;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Integrin beta {ECO:0000256|RuleBase:RU000633};
OS Seriola lalandi dorsalis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=1841481 {ECO:0000313|Ensembl:ENSSLDP00000005039.1, ECO:0000313|Proteomes:UP000261360};
RN [1] {ECO:0000313|Ensembl:ENSSLDP00000005039.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) 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}. 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 AlphaFoldDB; A0A3B4WK93; -.
DR Ensembl; ENSSLDT00000005202.1; ENSSLDP00000005039.1; ENSSLDG00000003954.1.
DR GeneTree; ENSGT01090000259987; -.
DR Proteomes; UP000261360; Unplaced.
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; 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 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 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..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..799
FT /note="Integrin beta"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017486120"
FT TRANSMEM 730..752
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 34..465
FT /note="Integrin beta subunit VWA"
FT /evidence="ECO:0000259|SMART:SM00187"
FT DOMAIN 641..729
FT /note="Integrin beta subunit tail"
FT /evidence="ECO:0000259|SMART:SM01242"
FT DOMAIN 753..799
FT /note="Integrin beta subunit cytoplasmic"
FT /evidence="ECO:0000259|SMART:SM01241"
FT DISULFID 35..45
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 38..75
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 48..64
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 207..213
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 261..301
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 435..693
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 463..467
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 478..490
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 487..526
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 492..501
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 503..517
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 532..537
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 534..569
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 539..554
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 556..561
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 575..580
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 577..608
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 582..591
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 593..600
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 614..619
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 616..662
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 621..631
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 634..637
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 641..650
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 647..724
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 666..701
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
SQ SEQUENCE 799 AA; 88596 MW; 817E2FA8CCEC25C7 CRC64;
MDLRLLLIAS LSAVLGGSWA QPEGSICIKA NAQSCGECIQ VAETCGWCSD ENFLTVGESK
SARCDDLESL KNRNCDVTKI ENPRGSITTD KNKPVTNRKK DMAEKLKPEQ ITQIQPQKLT
LTLRSGEPQT FELKFKRAED YPIDLYYLMD LSFSMKDDLE NVKNLGTDLM REMQEITSDF
RIGFGSFVEK TVMPYISTTP ARLINPCTGN QNCTSPFSYK NVLKLTENGD EFNRLVSQQQ
ISGNLDSPEG GFDAIMQVAV CEEHIGWRNV TRLLVFSTDA GFHFAGDGKL GGIVLPNDGK
CHLENNMYTM SHYYDYPSIA HLVQKLSDHN IQTIFAVTEE FQPVYKELKN LIPKSAVGTL
SSNSSNVIKL IIDAYNSLSS EVILENGRLP EGVSITYKSI CKNGVEGTGE NGRKCSNISI
GDEVSFRISI ESQKCPSHGK SEVIKIKPLG FTEEVEIVLN FICDCQCAAE GQPNSDKCHE
GNGTFECGAC KCNDGRIGRL CECSKDEVRT EDLDANCRKD NGTDICSNNG DCVCGTCECK
KRENPAEVYS GKYCECDNFN CDRSNNKLCG GHGRCECRKC ICDANYTGSA CDCSLETSTC
LAKNGQICNG RGTCECGICK CTNPKFQGPT CEICPTCPGV CAEHKDCVQC RAFDAGEKKD
TCEHECSYFE LIKVKDRDKL PQPTDQSFPL THCKERDAND CWFYYTYAIR NDTKEVYVVE
NLECPAGPDI IPIVAGVVAG IVLIGLALLL IWKLLMIIHD RREFAKFEKE KMNAKWDTGE
NPIYKSAVTT VVNPKYEGK
//
