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Database: UniProt
Entry: P12607
LinkDB: P12607
Original site: P12607 
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   13-FEB-2019, entry version 124.
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;
OC   Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
OC   Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2833505;
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
CC       receptor complexes that recognize the sequence R-G-D in a wide
CC       array of ligands. May be involved in osteoblast compaction (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit.
CC   -!- SUBCELLULAR LOCATION: Cell membrane
CC       {ECO:0000250|UniProtKB:P05556}; Single-pass type I membrane
CC       protein {ECO:0000255}. Cell projection, invadopodium membrane
CC       {ECO:0000250|UniProtKB:P05556}; Single-pass type I membrane
CC       protein {ECO:0000255}. Cell projection, ruffle membrane
CC       {ECO:0000250|UniProtKB:P05556}; Single-pass type I membrane
CC       protein {ECO:0000255}. Melanosome {ECO:0000250}. Cleavage furrow
CC       {ECO:0000250}. Cell projection, lamellipodium {ECO:0000250}. Cell
CC       projection, ruffle {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the integrin beta chain family.
CC       {ECO:0000305}.
DR   EMBL; M20180; AAA49890.1; -; mRNA.
DR   PIR; B28193; B28193.
DR   UniGene; Xl.7623; -.
DR   ProteinModelPortal; P12607; -.
DR   SMR; P12607; -.
DR   PRIDE; P12607; -.
DR   HOVERGEN; HBG006190; -.
DR   GO; GO:0030054; C:cell 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:0071438; C:invadopodium membrane; ISS:UniProtKB.
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   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; Phosphoprotein;
KW   Receptor; Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     21
FT   CHAIN        22    798       Integrin beta-1-B.
FT                                /FTId=PRO_0000016339.
FT   TOPO_DOM     22    727       Extracellular. {ECO:0000255}.
FT   TRANSMEM    728    751       Helical. {ECO:0000255}.
FT   TOPO_DOM    752    798       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      139    377       VWFA.
FT   REPEAT      466    515       I.
FT   REPEAT      516    559       II.
FT   REPEAT      560    598       III.
FT   REPEAT      599    635       IV.
FT   REGION      466    635       Cysteine-rich tandem repeats.
FT   MOD_RES     783    783       Phosphotyrosine. {ECO:0000250}.
FT   CARBOHYD    109    109       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    131    131       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    211    211       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    223    223       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    268    268       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    362    362       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    416    416       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    481    481       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    520    520       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    584    584       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    669    669       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     28    464       {ECO:0000250}.
FT   DISULFID     36     46       {ECO:0000250}.
FT   DISULFID     39     76       {ECO:0000250}.
FT   DISULFID     49     65       {ECO:0000250}.
FT   DISULFID    206    212       {ECO:0000250}.
FT   DISULFID    260    300       {ECO:0000250}.
FT   DISULFID    400    414       {ECO:0000250}.
FT   DISULFID    434    691       {ECO:0000250}.
FT   DISULFID    462    466       {ECO:0000250}.
FT   DISULFID    477    489       {ECO:0000250}.
FT   DISULFID    486    525       {ECO:0000250}.
FT   DISULFID    491    500       {ECO:0000250}.
FT   DISULFID    502    516       {ECO:0000250}.
FT   DISULFID    531    536       {ECO:0000250}.
FT   DISULFID    533    568       {ECO:0000250}.
FT   DISULFID    538    553       {ECO:0000250}.
FT   DISULFID    555    560       {ECO:0000250}.
FT   DISULFID    574    579       {ECO:0000250}.
FT   DISULFID    576    607       {ECO:0000250}.
FT   DISULFID    581    590       {ECO:0000250}.
FT   DISULFID    592    599       {ECO:0000250}.
FT   DISULFID    613    618       {ECO:0000250}.
FT   DISULFID    615    661       {ECO:0000250}.
FT   DISULFID    620    630       {ECO:0000250}.
FT   DISULFID    633    636       {ECO:0000250}.
FT   DISULFID    640    649       {ECO:0000250}.
FT   DISULFID    646    723       {ECO:0000250}.
FT   DISULFID    665    699       {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
//
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