ITB1A_XENLA
ID ITB1A_XENLA Reviewed; 798 AA.
AC P12606; Q6IRR8;
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-A;
DE Flags: Precursor;
GN Name=itgb1-a;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
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; M20140; AAA49889.1; -; mRNA.
DR EMBL; BC070558; AAH70558.1; -; mRNA.
DR PIR; A28193; A28193.
DR RefSeq; NP_001081286.1; NM_001087817.1.
DR AlphaFoldDB; P12606; -.
DR SMR; P12606; -.
DR PRIDE; P12606; -.
DR DNASU; 397755; -.
DR GeneID; 397755; -.
DR KEGG; xla:397755; -.
DR CTD; 397755; -.
DR Xenbase; XB-GENE-946731; itgb1.L.
DR OMA; NCVCGAC; -.
DR OrthoDB; 473040at2759; -.
DR Proteomes; UP000186698; Chromosome 6L.
DR Bgee; 397755; Expressed in egg cell and 19 other tissues.
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-A"
FT /id="PRO_0000016338"
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 76..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..635
FT /note="Cysteine-rich tandem repeats"
FT COMPBIAS 76..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; 88167 MW; 093522509B298531 CRC64;
MAHYPVFTVG LLTCLVLCIN AQQGGTECLK ANAKSCGECI QAGPNCGWCT KVDFLQEGEP
TSARCDDLAA LKSKGCPEDD IQNPRGRKQK LKDIPITSKG KGERMDPANI TQLRPQQMVF
ELRSGEPQTF NLTFRRAEDY PIDLYYLMDL SFSMKDDLEN VKSLGTALMT EMEKITSDFR
IGFGSFVEKT VMPYISTTPA KLINPCTSDQ NCTSPFSYKN VLNLTKDGKL FNDLVGKQQI
SGNLDSPEGG FDAIMQVAVC GEQIGWRNVT RLLVFSTDAG FHFAGDGKLG GIVLPNDGKC
HLHENMYTMS HYYDYPSIAH LVQKLSENNI QTIFAVTEDF QPVYQELKNL IPKSAVGTLS
SNSSNVIQLI IDSYNSLSSE LILENSKLPE GVTISYKSFC KNGVKGTGED GRKCSNISIG
DQVEFEISVT AHKCPKKGQA ESIKIKPLGF NEEVEIILQF LCECDCQDKG TPNSPECHFG
NGTFECGACR CNDGRIGKEC ECSTDEVNSE DMDAYCRREN SSEICSNNGD CICGQCVCKK
RDNPNEVYSG KYCECDNFNC DRSNGLICGG KGICKCRVCE CFPNYSGSAC DCSEDTSTCM
AKNGQICNGR GICDCGRCKC TDPKFQGPTC ELCQTCVGVC AEHKECVQCR AFQKGEKQDV
CMEQCMHFNI SLVDSREELP QPGQAEALTH CKEKDAEDCW FYFTYSVDSK NEVMVHVVKE
PECPSGPDII PIVAGVVAGI VLIGLALLLI WKLLMIIHDR REFAKFEKEK MNAKWDTGEN
PIYKSAVTTV VNPKYEGK
