ID A0A3P8THS9_AMPPE Unreviewed; 793 AA.
AC A0A3P8THS9;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 28-JAN-2026, entry version 31.
DE RecName: Full=Integrin beta {ECO:0000256|RuleBase:RU000633};
OS Amphiprion percula (Orange clownfish) (Lutjanus percula).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Amphiprion.
OX NCBI_TaxID=161767 {ECO:0000313|Ensembl:ENSAPEP00000023218.1, ECO:0000313|Proteomes:UP000265080};
RN [1] {ECO:0000313|Ensembl:ENSAPEP00000023218.1, ECO:0000313|Proteomes:UP000265080}
RP NUCLEOTIDE SEQUENCE.
RA Lehmann R.;
RT "Finding Nemo's genes: A chromosome-scale reference assembly of the genome
RT of the orange clownfish Amphiprion percula.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPEP00000023218.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSAPEP00000023218.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell junction {ECO:0000256|ARBA:ARBA00004282}.
CC Cell membrane {ECO:0000256|RuleBase:RU000633}; Single-pass type I
CC membrane protein {ECO:0000256|RuleBase:RU000633}. Cell projection,
CC lamellipodium membrane {ECO:0000256|ARBA:ARBA00004121}. Postsynaptic
CC cell membrane {ECO:0000256|ARBA:ARBA00035006}; Single-pass type I
CC membrane protein {ECO:0000256|ARBA:ARBA00035006}.
CC -!- SIMILARITY: Belongs to the integrin beta chain family.
CC {ECO:0000256|ARBA:ARBA00007449, ECO:0000256|RuleBase:RU000633}.
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DR AlphaFoldDB; A0A3P8THS9; -.
DR STRING; 161767.ENSAPEP00000023218; -.
DR Ensembl; ENSAPET00000023833.1; ENSAPEP00000023218.1; ENSAPEG00000016468.1.
DR GeneTree; ENSGT01150000286919; -.
DR OMA; AKWDTTH; -.
DR Proteomes; UP000265080; Chromosome 19.
DR GO; GO:0009986; C:cell surface; IEA:TreeGrafter.
DR GO; GO:0005925; C:focal adhesion; IEA:TreeGrafter.
DR GO; GO:0008305; C:integrin complex; IEA:TreeGrafter.
DR GO; GO:0031258; C:lamellipodium membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070051; F:fibrinogen binding; IEA:TreeGrafter.
DR GO; GO:0001968; F:fibronectin binding; IEA:TreeGrafter.
DR GO; GO:0005178; F:integrin binding; IEA:TreeGrafter.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; IEA:TreeGrafter.
DR GO; GO:0016477; P:cell migration; IEA:TreeGrafter.
DR GO; GO:0007160; P:cell-matrix adhesion; IEA:TreeGrafter.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0070527; P:platelet aggregation; IEA:TreeGrafter.
DR GO; GO:0030335; P:positive regulation of cell migration; IEA:UniProtKB-ARBA.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:UniProtKB-ARBA.
DR GO; GO:0045124; P:regulation of bone resorption; IEA:UniProtKB-ARBA.
DR GO; GO:0051049; P:regulation of transport; IEA:UniProtKB-ARBA.
DR FunFam; 1.20.5.100:FF:000002; Integrin beta; 1.
DR FunFam; 2.10.25.10:FF:000036; Integrin beta; 1.
DR FunFam; 2.10.25.10:FF:000075; Integrin beta; 1.
DR FunFam; 2.60.40.1510:FF:000004; Integrin beta; 1.
DR FunFam; 3.30.1680.10:FF:000002; Integrin beta; 1.
DR FunFam; 3.40.50.410:FF:000002; Integrin beta; 1.
DR FunFam; 4.10.1240.30:FF:000001; Integrin beta; 1.
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; EGF_integrin_1.
DR InterPro; IPR057073; EGF_integrin_2.
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; IPR057243; Integrin_I-EGF_CS.
DR InterPro; IPR016201; PSI.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR10082; INTEGRIN BETA SUBUNIT; 1.
DR PANTHER; PTHR10082:SF25; INTEGRIN BETA-3; 1.
DR Pfam; PF07974; EGF_2; 1.
DR Pfam; PF23105; EGF_integrin; 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; I_EGF_1; 1.
DR PROSITE; PS52047; I_EGF_2; 2.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
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|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR002512-1};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Integrin {ECO:0000256|ARBA:ARBA00023037, ECO:0000256|RuleBase:RU000633};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00023257};
KW Reference proteome {ECO:0000313|Proteomes:UP000265080};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Synapse {ECO:0000256|ARBA:ARBA00023018};
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..793
FT /note="Integrin beta"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018006230"
FT TRANSMEM 723..745
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 27..76
FT /note="PSI"
FT /evidence="ECO:0000259|SMART:SM00423"
FT DOMAIN 35..460
FT /note="Integrin beta subunit VWA"
FT /evidence="ECO:0000259|SMART:SM00187"
FT DOMAIN 638..722
FT /note="Integrin beta subunit tail"
FT /evidence="ECO:0000259|SMART:SM01242"
FT DOMAIN 746..792
FT /note="Integrin beta subunit cytoplasmic"
FT /evidence="ECO:0000259|SMART:SM01241"
FT DISULFID 28..460
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 36..46
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 39..75
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 49..64
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 202..209
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 257..298
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 399..411
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 431..685
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 458..462
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 473..485
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 482..525
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 487..496
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 531..536
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 533..566
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 538..551
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 553..558
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 572..577
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 574..605
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 579..588
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 590..597
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 611..616
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 613..661
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 618..628
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 631..634
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 638..647
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 644..717
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 665..693
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
SQ SEQUENCE 793 AA; 86754 MW; DDF4E6C0722A2AF7 CRC64;
MGALLTHSMF FWILFCTGIT AVCGSNVCTS RGASTCKQCL AVHPSCAWCF QEDFGQGVAG
SSRCDLKTNL VAAGCATSAL ESPTSKLQVI EDRPLSNKAA GAAQVTQIKP QKLHITLRPD
DAKRFTVKVR QVEDYPVDLY YLMDLSYSMN DDLFRLRTLG RGLAEAMNRT TSNLRMGFGA
FVDKPLSPYM YISPKEAVKN PCYSINTTCL PQFGYKHVLS LTEEVGRFTE EVKKQMVSRN
RDAPEGGFDA IIQAAVCKEQ IGWRPGASHL LIFTSDAKTH VALDGRLAGI VQPNDGRCHL
NSENMYSMST TMDYPSLALI TEKMSENNIN LIFAVTNPVV PLYQNYSELI PGTTVGTLSN
DSGNVIQLIL KAYAKIRSKV ELELQDVPEE LSLSFNATCL NGELIPGLKS CSGLKIGDTV
SFSVEARARG CPKQKKKTFV IKPVGFKDSL SITVTFECDC KCQAKAQPNS PKCSQGNGTY
ECGICQCHPG RLGPHCECAE GDYNPTEQDR CSGPAGTGGS QSAICSGRGD CVCGQCVCHS
SDFGKVWGKL CECDDFNCLR YKGELCSGHG VCNCGFCQCA PDWQGENCNC SRRTDTCMSS
LGLLCSGRGQ CICGACECTQ PGAYGATCDK CPTCPDACTM KKECVECKHF KRGRLFEDNT
CSRICKDEIM LVDELVLHDT NAVNCTYKDE DDCVERFQYY EDASGKSILF VVKEPDCPKG
PDILVVLLSV AGAILFLGLA ALLIWKLLVT IHDRREFAKF EEERARAKWD TGHNPLYKGA
TSTFTNITYR GKD
//
