ITB1B_XENLA
ID ITB1B_XENLA Reviewed; 798 AA.
AC P12607;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Integrin beta-1-B;
DE AltName: Full=Integrin beta-1*;
DE Flags: Precursor;
GN Name=itgb1-b;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2833505; DOI=10.1016/s0021-9258(18)60720-3;
RA Desimone D.W., Hynes R.O.;
RT "Xenopus laevis integrins. Structural conservation and evolutionary
RT divergence of integrin beta subunits.";
RL J. Biol. Chem. 263:5333-5340(1988).
CC -!- FUNCTION: Beta integrins associate with alpha subunits to form receptor
CC complexes that recognize the sequence R-G-D in a wide array of ligands.
CC May be involved in osteoblast compaction (By similarity). May play role
CC in myoblast differentiation and fusion during skeletal myogenesis (By
CC similarity). {ECO:0000250|UniProtKB:P05556,
CC ECO:0000250|UniProtKB:P07228}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P05556};
CC Single-pass type I membrane protein {ECO:0000255}. Cell projection,
CC invadopodium membrane {ECO:0000250|UniProtKB:P05556}; Single-pass type
CC I membrane protein {ECO:0000255}. Cell projection, ruffle membrane
CC {ECO:0000250|UniProtKB:P05556}; Single-pass type I membrane protein
CC {ECO:0000255}. Melanosome {ECO:0000250}. Cleavage furrow {ECO:0000250}.
CC Cell projection, lamellipodium {ECO:0000250}. Cell projection, ruffle
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the integrin beta chain family. {ECO:0000305}.
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DR EMBL; M20180; AAA49890.1; -; mRNA.
DR PIR; B28193; B28193.
DR AlphaFoldDB; P12607; -.
DR SMR; P12607; -.
DR PRIDE; P12607; -.
DR Proteomes; UP000186698; Genome assembly.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR GO; GO:0008305; C:integrin complex; IEA:InterPro.
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:0038023; F:signaling receptor activity; IEA:InterPro.
DR GO; GO:0007160; P:cell-matrix adhesion; IEA:InterPro.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
DR GO; GO:0045445; P:myoblast differentiation; ISS:UniProtKB.
DR GO; GO:0007520; P:myoblast fusion; ISS:UniProtKB.
DR Gene3D; 3.40.50.410; -; 1.
DR InterPro; IPR013111; EGF_extracell.
DR InterPro; IPR040622; I-EGF_1.
DR InterPro; IPR027071; Integrin_beta-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; PTHR10082; 1.
DR PANTHER; PTHR10082:SF28; PTHR10082:SF28; 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 SMART; SM00423; PSI; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR SUPFAM; SSF69179; SSF69179; 1.
DR SUPFAM; SSF69687; SSF69687; 1.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS00243; INTEGRIN_BETA; 3.
PE 2: Evidence at transcript level;
KW Cell adhesion; Cell junction; Cell membrane; Cell projection;
KW Disulfide bond; Glycoprotein; Integrin; Membrane; Myogenesis;
KW Phosphoprotein; Receptor; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT CHAIN 22..798
FT /note="Integrin beta-1-B"
FT /id="PRO_0000016339"
FT TOPO_DOM 22..727
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 728..751
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 752..798
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 139..377
FT /note="VWFA"
FT REPEAT 466..515
FT /note="I"
FT REPEAT 516..559
FT /note="II"
FT REPEAT 560..598
FT /note="III"
FT REPEAT 599..635
FT /note="IV"
FT REGION 77..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..635
FT /note="Cysteine-rich tandem repeats"
FT COMPBIAS 77..100
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 783
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 131
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 223
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 268
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 362
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 416
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 481
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 520
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 584
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 669
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 28..464
FT /evidence="ECO:0000250"
FT DISULFID 36..46
FT /evidence="ECO:0000250"
FT DISULFID 39..76
FT /evidence="ECO:0000250"
FT DISULFID 49..65
FT /evidence="ECO:0000250"
FT DISULFID 206..212
FT /evidence="ECO:0000250"
FT DISULFID 260..300
FT /evidence="ECO:0000250"
FT DISULFID 400..414
FT /evidence="ECO:0000250"
FT DISULFID 434..691
FT /evidence="ECO:0000250"
FT DISULFID 462..466
FT /evidence="ECO:0000250"
FT DISULFID 477..489
FT /evidence="ECO:0000250"
FT DISULFID 486..525
FT /evidence="ECO:0000250"
FT DISULFID 491..500
FT /evidence="ECO:0000250"
FT DISULFID 502..516
FT /evidence="ECO:0000250"
FT DISULFID 531..536
FT /evidence="ECO:0000250"
FT DISULFID 533..568
FT /evidence="ECO:0000250"
FT DISULFID 538..553
FT /evidence="ECO:0000250"
FT DISULFID 555..560
FT /evidence="ECO:0000250"
FT DISULFID 574..579
FT /evidence="ECO:0000250"
FT DISULFID 576..607
FT /evidence="ECO:0000250"
FT DISULFID 581..590
FT /evidence="ECO:0000250"
FT DISULFID 592..599
FT /evidence="ECO:0000250"
FT DISULFID 613..618
FT /evidence="ECO:0000250"
FT DISULFID 615..661
FT /evidence="ECO:0000250"
FT DISULFID 620..630
FT /evidence="ECO:0000250"
FT DISULFID 633..636
FT /evidence="ECO:0000250"
FT DISULFID 640..649
FT /evidence="ECO:0000250"
FT DISULFID 646..723
FT /evidence="ECO:0000250"
FT DISULFID 665..699
FT /evidence="ECO:0000250"
SQ SEQUENCE 798 AA; 88303 MW; A1C45EA3711CF7C7 CRC64;
MARYPVFTFV FLICLVLCTN AQQGGTECLK ANAKSCGECI QAGPNCGWCT KVDFLQEGEP
TSARCDDLAA LKTKGCPEDD IQNPRGRKQK LKDIPITSKG KGERMDPANI TQLRPQQLVF
ELRSGEPQTF NLTFRRAEDY PIDLYYLMDL SFSMKDDLEN VKSLGTALMT EMEKITSDFR
IGFGSFVEKT VMPYISTTPA KLLNPCTNDQ NCTSPFSYKN VLNLTKDGKL FNDLVGKQQI
SGNLDSPEGG FDAIMQVAVC GEQIGWRNVT RLLVFSTDAG FHFAGDGKLG GIVLPNDGRC
HLHGNMYTMS HYYDYPSIAH LVQKLSENNI QTIFAVTEDF QPVYQELKNL IPKSAVGTLS
SNSSNVIQLI IDSYNSLSSE LILENSKLPE GVTISYRSFC KNGVKGTGED GRKCSNISIG
DQVEFEISVT AHKCPKKGQA ESIKIKPLGF NEEVEIVLQF ICECDCQDKG TPNSPECHFG
NGTFECGACR CNEGRIGKEC ECSTDEVNSE DMDAYCRREN SSEICSNNGD CICGQCVCKK
RDNPNEVYSG KYCECDNFNC DRSNGLICGG KGVCKCRVCE CFPNYSGSAC DCSEDTSTCM
AKNGQICNGR GICDCGRCKC TDPKFQGPTC ELCQTCVGVC TEHKECVQCR AFQKGEKQDV
CMEQCMHFNI SLVDSREELP QPGQAEALTH CKEKDAEDCW FYFTYSVDSK NEVMVHVVKE
PECPSGPDII PIVAGVVAGI VLIGLALLLI WKLLMIIHDR REFAKFEKEK MNAKWDTGEN
PIYKSAVATV VNPKYEGK
