ID A0A3Q3W8Y1_MOLML Unreviewed; 778 AA.
AC A0A3Q3W8Y1;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Integrin beta {ECO:0000256|RuleBase:RU000633};
OS Mola mola (Ocean sunfish) (Tetraodon mola).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Molidae; Mola.
OX NCBI_TaxID=94237 {ECO:0000313|Ensembl:ENSMMOP00000008357.1, ECO:0000313|Proteomes:UP000261620};
RN [1] {ECO:0000313|Ensembl:ENSMMOP00000008357.1}
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}.
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; A0A3Q3W8Y1; -.
DR STRING; 94237.ENSMMOP00000008357; -.
DR Ensembl; ENSMMOT00000008509.1; ENSMMOP00000008357.1; ENSMMOG00000006467.1.
DR OMA; TNCECQC; -.
DR Proteomes; UP000261620; 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; 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; 3.
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; 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; 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; 1.
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; 2.
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:UP000261620};
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..778
FT /note="Integrin beta"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018596388"
FT TRANSMEM 709..735
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 24..74
FT /note="PSI"
FT /evidence="ECO:0000259|SMART:SM00423"
FT DOMAIN 32..454
FT /note="Integrin beta subunit VWA"
FT /evidence="ECO:0000259|SMART:SM00187"
FT DOMAIN 626..708
FT /note="Integrin beta subunit tail"
FT /evidence="ECO:0000259|SMART:SM01242"
FT DOMAIN 732..778
FT /note="Integrin beta subunit cytoplasmic"
FT /evidence="ECO:0000259|SMART:SM01241"
FT DISULFID 33..43
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 36..73
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 46..62
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 198..205
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 253..294
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 394..407
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 427..670
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 452..456
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 475..513
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 480..489
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 491..505
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 519..524
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 521..555
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 526..540
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 542..547
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 561..566
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 563..594
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 568..577
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 579..586
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 600..605
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 602..647
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 607..616
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 619..622
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 626..635
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 632..703
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 651..678
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
SQ SEQUENCE 778 AA; 86339 MW; 66CD3024BE4226A3 CRC64;
MDCWPLLILL LLICKNGLCQ NEEVCSKTVI NSCSDCIRSG PHCVWCKQLN FTKPGEQEAV
RCDTRAQLMQ RGCQMDEIIS PENRISIVKE TPLSISFNQQ EPVQLSPQNI SLKIRPGHST
TFSVSFKRVQ GYPVDLYYLM DLSNSMKDDL DNVKGLGKDL FEALKIITEH AQIGFGAFVD
KTVLPYTNTN EKKLKRPCDE DTQQCQAAFS YRHVLNMTPS EDEFKRKVTE QFISGNLDSP
EGSLDAIMQA AVCGDIIGWR NSSTRLIVLT TDAGFHMAGD GKLAGILEPN DGHCHMKNNL
YYKSIDMDYP SVGQLAMQLE KNNIQPIFAV TENVESVYKQ LSKMIPKSEV GVLQKDSKNV
VELIKSAYNR LSSKVTLTHD NLPDNVKVVY TPKCKHAGPP GSSEGVCGNV PAGEKISFEV
TVVADSCMKD KSFTIRPLGI KDTLTVSLST NCECDCNDPQ DSTHPHCKGK GRVNCGICSC
SEGSVGQFCE CSTGDKDEHF LRASCQRDNG TECEGRGDCV CGRCKCHTTE NGKFYHGDFC
ECDDEHCEKF QNKLCGGNGK CNCGKCECYQ DYEGSACQCR VSDEGCRTLE NTVCYGRGIC
KCNRCECNEG YQRPRCKTCL GCPDPCQTKL NCIECLGFDS GPFEKNCSVA CSSSIHSEMV
EEFTIASKQC QQKDSQGCWI KFNLEQLVGE DNYNAEILKE RDCPQPPNIT AIIGGSIASV
AFLGILLLML IKLLIYMNDL KEYKKFEKEK KKSKWAEANN PLFQDATTTI ANPTFTGE
//
