ID A0A3Q1I2U2_ANATE Unreviewed; 786 AA.
AC A0A3Q1I2U2;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Integrin beta {ECO:0000256|RuleBase:RU000633};
GN Name=ITGB1 {ECO:0000313|Ensembl:ENSATEP00000015747.2};
OS Anabas testudineus (Climbing perch) (Anthias testudineus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000015747.2, ECO:0000313|Proteomes:UP000265040};
RN [1] {ECO:0000313|Ensembl:ENSATEP00000015747.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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; A0A3Q1I2U2; -.
DR STRING; 64144.ENSATEP00000015747; -.
DR Ensembl; ENSATET00000015991.2; ENSATEP00000015747.2; ENSATEG00000010857.2.
DR GeneTree; ENSGT01090000259987; -.
DR Proteomes; UP000265040; 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 Reference proteome {ECO:0000313|Proteomes:UP000265040};
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..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..786
FT /note="Integrin beta"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5030079692"
FT TRANSMEM 717..739
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 21..452
FT /note="Integrin beta subunit VWA"
FT /evidence="ECO:0000259|SMART:SM00187"
FT DOMAIN 628..716
FT /note="Integrin beta subunit tail"
FT /evidence="ECO:0000259|SMART:SM01242"
FT DOMAIN 740..786
FT /note="Integrin beta subunit cytoplasmic"
FT /evidence="ECO:0000259|SMART:SM01241"
FT DISULFID 22..32
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 25..62
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 35..51
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 194..200
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 248..288
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 422..680
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 450..454
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 465..477
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 474..513
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 479..488
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 490..504
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 519..524
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 521..556
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 526..541
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 543..548
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 562..567
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 564..595
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 569..578
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 580..587
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 601..606
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 603..649
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 608..618
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 621..624
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 628..637
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 634..711
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 653..688
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
SQ SEQUENCE 786 AA; 87301 MW; 8A2558557DDA913A CRC64;
VNCLELFSAS LSICIKANAQ SCGECIQVSE TCGWCTDENF LTVGESKSAR CDDLESLKKR
NCNEAKIENP RGGVTIDKDK PVTDRKKDKA EKLKPEQITQ IQPQKLTVTL RSDEPQTFRL
KFKRAEDYPI DLYYLMDLSF SMEDDLENLK NLGTDLMKEM QAITSDFRIG FGSFVEKTVM
PYISTTPARL INPCTGNQNC TSPFSYKNVL KLTNNGAEFN RLVSQQQISG NLDSPEGGFD
AIMQVAVCEE QIGWRNVTRL LVFSTDAGFH FAGDGKLGGI VLPNDGKCHL ENNIYTMSHY
YDYPSIAHLV QKLSDHNIQT IFAVTEEFQP VYKELKNLIP KSAVGTLSSN SSNVIKLIID
AYNSLSSEVI LENGRLPEGV SITYKSICKN DVVGTGENGR KCSNISIGDE VYFNISIESK
KCPSNGKSEI IKIKPLGFTE EVELVLNFIC DCQCASKGEP NSAKCHEGYG TFECGACKCN
EGRIGRVCEC SKDEVRTEDL DANCRKDNGT DICSNNGDCV CGTCECKKRE NPAEVYSGKY
CECDNFNCDR SNNKLCGGHG RCECRKCICD TNYTGSACDC SLDTTSCLAK NGQICNGRGT
CECGSCKCTN AKFQGPTCEI CPTCPGVCAE HKECVQCRAF KAGEKKSTCE QDCKYFNLIT
VKDRENLPQP TDQSFPLTHC KERDANDCWF YYTYAVRNDT KEVYVVEKLD CPRGPDIIPI
VAGVVAGIVL IGLALLLIWK LLMIIHDRRE FAKFEKEKMN AKWDTGENPI YKSAVTTVVN
PKYEGK
//
