ID A0A3B4DQ66_PYGNA Unreviewed; 745 AA.
AC A0A3B4DQ66;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Integrin beta {ECO:0000256|RuleBase:RU000633};
GN Name=ITGB6 {ECO:0000313|Ensembl:ENSPNAP00000025251.1};
OS Pygocentrus nattereri (Red-bellied piranha).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Pygocentrus.
OX NCBI_TaxID=42514 {ECO:0000313|Ensembl:ENSPNAP00000025251.1, ECO:0000313|Proteomes:UP000261440};
RN [1] {ECO:0000313|Ensembl:ENSPNAP00000025251.1}
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}.
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}.
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DR AlphaFoldDB; A0A3B4DQ66; -.
DR Ensembl; ENSPNAT00000008076.1; ENSPNAP00000025251.1; ENSPNAG00000010320.1.
DR GeneTree; ENSGT01100000263555; -.
DR Proteomes; UP000261440; Unplaced.
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; 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; IPR040622; I-EGF_1.
DR InterPro; IPR033760; Integrin_beta_N.
DR InterPro; IPR015812; Integrin_bsu.
DR InterPro; IPR014836; Integrin_bsu_cyt_dom.
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:SF11; INTEGRIN BETA-6; 1.
DR Pfam; PF18372; I-EGF_1; 1.
DR Pfam; PF08725; Integrin_b_cyt; 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; SM00423; PSI; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 2.
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 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};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000633};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 22..68
FT /note="PSI"
FT /evidence="ECO:0000259|SMART:SM00423"
FT DOMAIN 27..449
FT /note="Integrin beta subunit VWA"
FT /evidence="ECO:0000259|SMART:SM00187"
FT DOMAIN 691..737
FT /note="Integrin beta subunit cytoplasmic"
FT /evidence="ECO:0000259|SMART:SM01241"
FT DISULFID 28..38
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 31..67
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 41..56
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 192..199
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 247..288
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 389..401
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 421..641
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 447..451
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 462..474
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 471..495
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 476..485
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 501..506
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 503..536
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 508..521
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 523..528
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 542..547
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 544..575
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 549..558
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 581..586
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 588..598
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 601..604
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 620..649
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
SQ SEQUENCE 745 AA; 81830 MW; 5B0A96B61F0DC05C CRC64;
NHFCLVCSCL SAIKKPKPCS GTCSALTCDA CVQLGPQCAW CTLQNFTVSL ADGERCGTLE
ELRARGCAGE AVEFPVTRAE LLEDEPLGRR AGRANVSHIA PQRMALRLRP GTRVTFQVKV
LQPKDHPVDM YYLMDLSASM IDDLERITQL GSTLSKEMAN LTSKFRLGFG SFVEKPILPY
IKTTPEELAN PCRSVDYVCL PTFGYRHILP LTSSMDEFNK IISKQRVSAN NDIPECGFDA
IMQAAVCGDK IGWRNDSMRL LVFASDADSH FGMDSKMAGI VIPNDGQCHL DSNNEYSMAG
HLEYPTLGQL VDKLVENNIL LIFAVTANQR QNYENYANLI PGATVGVLEN DSRNILELIM
TAYKELRSEI EMEVLGDTEH LQISFTALCQ DGKVDQGMKR CTNVKVGDTV AFNVTVELGS
CLDGPRHFSL RPVGFQDTLE VELESLCACD CHRTAEPNSI YCSDGQGALD CGLCMCDPGF
MGPKCECEER EAEMCSGQGE CFCGLCLCHQ SSFGHVYGKY CECDDFSCLR FRGKLCGGNG
MCDCGECVCH SGWTGEYCNC STSMRACESA DGSVCSGRGK CVCGKCECSV PGASGDKCEK
CLTCGDICSR TRYRHTTVFC SDIYNITERQ EDFEESRAVL CTLQNENECL ISFALATSDK
ECPKAPNIAM IALGVCMSVL TIGITLLVVW KLLVSVHDRK EVAKFEAERA KAKWQSGTNP
LFRSSTSTFK NVAYKNTGRQ KVDIC
//
