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Integrin beta-1 (Fibronectin receptor subunit beta) (VLA-4 subunit beta) (CD antigen CD29)

 ITB1_FELCA              Reviewed;         798 AA.
P53713;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
23-MAY-2018, entry version 136.
RecName: Full=Integrin beta-1;
AltName: Full=Fibronectin receptor subunit beta;
AltName: Full=VLA-4 subunit beta;
AltName: CD_antigen=CD29;
Flags: Precursor;
Name=ITGB1;
Felis catus (Cat) (Felis silvestris catus).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae;
Felinae; Felis.
NCBI_TaxID=9685;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=T lymphoblast;
Willett B.J.;
Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Integrins alpha-1/beta-1, alpha-2/beta-1, alpha-10/beta-
1 and alpha-11/beta-1 are receptors for collagen. Integrins alpha-
1/beta-1 and alpha-2/beta-2 recognize the proline-hydroxylated
sequence G-F-P-G-E-R in collagen. Integrins alpha-2/beta-1, alpha-
3/beta-1, alpha-4/beta-1, alpha-5/beta-1, alpha-8/beta-1, alpha-
10/beta-1, alpha-11/beta-1 and alpha-V/beta-1 are receptors for
fibronectin. Alpha-4/beta-1 recognizes one or more domains within
the alternatively spliced CS-1 and CS-5 regions of fibronectin.
Integrin alpha-5/beta-1 is a receptor for fibrinogen. Integrin
alpha-1/beta-1, alpha-2/beta-1, alpha-6/beta-1 and alpha-7/beta-1
are receptors for lamimin. Integrin alpha-4/beta-1 is a receptor
for VCAM1 and recognizes the sequence Q-I-D-S in VCAM1. Integrin
alpha-9/beta-1 is a receptor for VCAM1, cytotactin and
osteopontin. It recognizes the sequence A-E-I-D-G-I-E-L in
cytotactin. Integrin alpha-3/beta-1 is a receptor for epiligrin,
thrombospondin and CSPG4. Integrin alpha-3/beta-1 provides a
docking site for FAP (seprase) at invadopodia plasma membranes in
a collagen-dependent manner and hence may participate in the
adhesion, formation of invadopodia and matrix degradation
processes, promoting cell invasion. Alpha-3/beta-1 may mediate
with LGALS3 the stimulation by CSPG4 of endothelial cells
migration. Integrin alpha-V/beta-1 is a receptor for vitronectin.
Beta-1 integrins recognize the sequence R-G-D in a wide array of
ligands. When associated with alpha-7/beta-1 integrin, regulates
cell adhesion and laminin matrix deposition. Involved in promoting
endothelial cell motility and angiogenesis. Involved in osteoblast
compaction through the fibronectin fibrillogenesis cell-mediated
matrix assembly process and the formation of mineralized bone
nodules. May be involved in up-regulation of the activity of
kinases such as PKC via binding to KRT1. Together with KRT1 and
RACK1, serves as a platform for SRC activation or inactivation.
Plays a mechanistic adhesive role during telophase, required for
the successful completion of cytokinesis. ITGA4:ITGB1 binds to
fractalkine (CX3CL1) and may act as its coreceptor in CX3CR1-
dependent fractalkine signaling. ITGA4:ITGB1 and ITGA5:ITGB1 bind
to PLA2G2A via a site (site 2) which is distinct from the
classical ligand-binding site (site 1) and this induces integrin
conformational changes and enhanced ligand binding to site 1.
ITGA5:ITGB1 acts as a receptor for fibrillin-1 (FBN1) and mediates
R-G-D-dependent cell adhesion to FBN1. ITGA5:ITGB1 is a receptor
for IL1B and binding is essential for IL1B signaling.
{ECO:0000250|UniProtKB:P05556}.
-!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Beta-1
associates with either alpha-1, alpha-2, alpha-3, alpha-4, alpha-
5, alpha-6, alpha-7, alpha-8, alpha-9, alpha-10, alpha-11 or
alpha-V. Binds LGALS3BP and NMRK2, when associated with alpha-7,
but not with alpha-5. Interacts with FLNA, FLNB, FLNC and RANBP9.
Interacts with KRT1 in the presence of RACK1 and SRC. Interacts
with JAML; integrin alpha-4/beta-1 may regulate leukocyte to
endothelial cells adhesion by controlling JAML homodimerization.
Interacts with RAB21. Interacts (via the cytoplasmic region) with
RAB25 (via the hypervariable C-terminal region). Interacts with
FGR and HCK. Interacts with MYO10. Interacts with DAB2. Interacts
with ITGB1BP1 (via C-terminal region); the interaction is a
prerequisite for focal adhesion disassembly. Interacts with
FERMT2; the interaction is inhibited in presence of ITGB1BP1.
Interacts with TLN1; the interaction is prevented by competitive
binding of ITGB1BP1. Interacts with ACAP1; required for ITGB1
recycling. Interacts with ASAP3. Interacts with seprase FAP
(seprase); the interaction occurs at the cell surface of
invadopodia membrane in a collagen-dependent manner. Interacts
with EMP2; the interaction may be direct or indirect and ITGB1 has
a heterodimer form (By similarity). ITGA5:ITGB1 interacts with
NOV. ITGA4:ITGB1 is found in a ternary complex with CX3CR1 and
CX3CL1. ITGA5:ITGB1 interacts with FBN1. ITGA5:ITGB1 interacts
with IL1B. {ECO:0000250|UniProtKB:P05556,
ECO:0000250|UniProtKB:P09055}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P05556}; Single-pass type I membrane
protein {ECO:0000255}. Cell projection, invadopodium membrane
{ECO:0000250|UniProtKB:P05556}; Single-pass type I membrane
protein {ECO:0000255}. Cell projection, ruffle membrane
{ECO:0000250|UniProtKB:P05556}; Single-pass type I membrane
protein {ECO:0000255}. Recycling endosome
{ECO:0000250|UniProtKB:P05556}. Melanosome
{ECO:0000250|UniProtKB:P05556}. Cell projection, lamellipodium
{ECO:0000250|UniProtKB:P05556}. Cell projection, ruffle
{ECO:0000250|UniProtKB:P05556}. Cell junction, focal adhesion
{ECO:0000250|UniProtKB:P05556}. Cell surface
{ECO:0000250|UniProtKB:P05556}. Note=Enriched preferentially at
invadopodia, cell membrane protrusions that correspond to sites of
cell invasion, in a collagen-dependent manner. Localized at plasma
and ruffle membranes in a collagen-independent manner. Colocalizes
with ITGB1BP1 and metastatic suppressor protein NME2 at the edge
or peripheral ruffles and lamellipodia during the early stages of
cell spreading on fibronectin or collagen. Translocates from
peripheral focal adhesions to fibrillar adhesions in an ITGB1BP1-
dependent manner. {ECO:0000250|UniProtKB:P05556}.
-!- PTM: The cysteine residues are involved in intrachain disulfide
bonds. {ECO:0000250}.
-!- SIMILARITY: Belongs to the integrin beta chain family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U27351; AAC19407.1; -; mRNA.
RefSeq; NP_001041625.1; NM_001048160.2.
ProteinModelPortal; P53713; -.
SMR; P53713; -.
STRING; 9685.ENSFCAP00000016197; -.
PRIDE; P53713; -.
GeneID; 751821; -.
KEGG; fca:751821; -.
CTD; 3688; -.
eggNOG; KOG1226; Eukaryota.
eggNOG; ENOG410XP60; LUCA.
HOVERGEN; HBG006190; -.
InParanoid; P53713; -.
KO; K05719; -.
Proteomes; UP000011712; Unplaced.
GO; GO:0009986; C:cell surface; ISS:UniProtKB.
GO; GO:0005925; C:focal adhesion; ISS:UniProtKB.
GO; GO:0008305; C:integrin complex; IEA:InterPro.
GO; GO:0071438; C:invadopodium membrane; ISS:UniProtKB.
GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; ISS:UniProtKB.
GO; GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell.
GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
GO; GO:0038023; F:signaling receptor activity; IEA:InterPro.
GO; GO:0033627; P:cell adhesion mediated by integrin; ISS:UniProtKB.
GO; GO:0007160; P:cell-matrix adhesion; IEA:InterPro.
GO; GO:0071404; P:cellular response to low-density lipoprotein particle stimulus; ISS:UniProtKB.
GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISS:UniProtKB.
GO; GO:0031623; P:receptor internalization; ISS:UniProtKB.
GO; GO:0010710; P:regulation of collagen catabolic process; ISS:UniProtKB.
Gene3D; 3.40.50.410; -; 1.
InterPro; IPR013111; EGF_extracell.
InterPro; IPR027071; Integrin_beta-1.
InterPro; IPR033760; Integrin_beta_N.
InterPro; IPR015812; Integrin_bsu.
InterPro; IPR014836; Integrin_bsu_cyt_dom.
InterPro; IPR012896; Integrin_bsu_tail.
InterPro; IPR036349; Integrin_bsu_tail_dom_sf.
InterPro; IPR002369; Integrin_bsu_VWA.
InterPro; IPR032695; Integrin_dom_sf.
InterPro; IPR016201; PSI.
InterPro; IPR036465; vWFA_dom_sf.
PANTHER; PTHR10082; PTHR10082; 1.
PANTHER; PTHR10082:SF28; PTHR10082:SF28; 1.
Pfam; PF07974; EGF_2; 1.
Pfam; PF08725; Integrin_b_cyt; 1.
Pfam; PF07965; Integrin_B_tail; 1.
Pfam; PF00362; Integrin_beta; 1.
Pfam; PF17205; PSI_integrin; 1.
PIRSF; PIRSF002512; Integrin_B; 1.
PRINTS; PR01186; INTEGRINB.
SMART; SM00187; INB; 1.
SMART; SM01241; Integrin_b_cyt; 1.
SMART; SM01242; Integrin_B_tail; 1.
SMART; SM00423; PSI; 1.
SUPFAM; SSF53300; SSF53300; 1.
SUPFAM; SSF69179; SSF69179; 1.
SUPFAM; SSF69687; SSF69687; 1.
PROSITE; PS00022; EGF_1; 2.
PROSITE; PS00243; INTEGRIN_BETA; 3.
2: Evidence at transcript level;
Acetylation; Cell adhesion; Cell junction; Cell membrane;
Cell projection; Complete proteome; Disulfide bond; Endosome;
Glycoprotein; Integrin; Isopeptide bond; Magnesium; Membrane;
Metal-binding; Phosphoprotein; Receptor; Reference proteome; Repeat;
Signal; Transmembrane; Transmembrane helix; Ubl conjugation.
SIGNAL 1 20 {ECO:0000250}.
CHAIN 21 798 Integrin beta-1.
/FTId=PRO_0000016333.
TOPO_DOM 21 728 Extracellular. {ECO:0000255}.
TRANSMEM 729 751 Helical. {ECO:0000255}.
TOPO_DOM 752 798 Cytoplasmic. {ECO:0000255}.
DOMAIN 140 378 VWFA.
REPEAT 466 515 I.
REPEAT 516 559 II.
REPEAT 560 598 III.
REPEAT 599 635 IV.
REGION 207 213 CX3CL1-binding.
{ECO:0000250|UniProtKB:P05556}.
REGION 295 314 CX3CL1-binding.
{ECO:0000250|UniProtKB:P05556}.
REGION 466 635 Cysteine-rich tandem repeats.
REGION 762 767 Signal for sorting from recycling
endosomes; interaction with ACAP1.
{ECO:0000250}.
REGION 785 792 Interaction with ITGB1BP1. {ECO:0000250}.
METAL 152 152 Magnesium. {ECO:0000250}.
METAL 154 154 Calcium 1; via carbonyl oxygen.
{ECO:0000250}.
METAL 156 156 Calcium 1. {ECO:0000250}.
METAL 157 157 Calcium 1. {ECO:0000250}.
METAL 189 189 Calcium 2. {ECO:0000250}.
METAL 244 244 Calcium 2. {ECO:0000250}.
METAL 246 246 Calcium 2. {ECO:0000250}.
METAL 248 248 Calcium 2; via carbonyl oxygen.
{ECO:0000250}.
METAL 249 249 Calcium 2. {ECO:0000250}.
METAL 249 249 Magnesium. {ECO:0000250}.
METAL 362 362 Calcium 1; via carbonyl oxygen.
{ECO:0000250}.
MOD_RES 777 777 Phosphothreonine.
{ECO:0000250|UniProtKB:P05556}.
MOD_RES 783 783 Phosphotyrosine.
{ECO:0000250|UniProtKB:P05556}.
MOD_RES 785 785 Phosphoserine.
{ECO:0000250|UniProtKB:P05556}.
MOD_RES 789 789 Phosphothreonine.
{ECO:0000250|UniProtKB:P05556}.
MOD_RES 794 794 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P05556}.
CARBOHYD 50 50 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 94 94 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 97 97 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 212 212 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 269 269 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 363 363 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 406 406 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 417 417 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 481 481 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 520 520 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 584 584 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 669 669 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 27 45 {ECO:0000250}.
DISULFID 35 464 {ECO:0000250}.
DISULFID 38 75 {ECO:0000250}.
DISULFID 48 64 {ECO:0000250}.
DISULFID 207 213 {ECO:0000250}.
DISULFID 261 301 {ECO:0000250}.
DISULFID 401 415 {ECO:0000250}.
DISULFID 435 462 {ECO:0000250}.
DISULFID 466 691 {ECO:0000250}.
DISULFID 477 489 {ECO:0000250}.
DISULFID 486 525 {ECO:0000250}.
DISULFID 491 500 {ECO:0000250}.
DISULFID 502 516 {ECO:0000250}.
DISULFID 531 536 {ECO:0000250}.
DISULFID 533 568 {ECO:0000250}.
DISULFID 538 553 {ECO:0000250}.
DISULFID 555 560 {ECO:0000250}.
DISULFID 574 579 {ECO:0000250}.
DISULFID 576 607 {ECO:0000250}.
DISULFID 581 590 {ECO:0000250}.
DISULFID 592 599 {ECO:0000250}.
DISULFID 613 618 {ECO:0000250}.
DISULFID 615 661 {ECO:0000250}.
DISULFID 620 630 {ECO:0000250}.
DISULFID 633 636 {ECO:0000250}.
DISULFID 640 649 {ECO:0000250}.
DISULFID 646 723 {ECO:0000250}.
DISULFID 665 699 {ECO:0000250}.
CROSSLNK 794 794 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate.
{ECO:0000250|UniProtKB:P05556}.
SEQUENCE 798 AA; 88093 MW; 2A1C38771046D838 CRC64;
MNLQLIFWIG LISSICCVFG QADENRCLKA NAKSCGECIQ AGPNCGWCVN STFLQEGMPT
SARCDDLEAL KKKGCHPDDI ENPRGSKDVK KNKNVTNRSK GTAEKLQPED ITQIQPQQLV
LQLRSGEPQT FTLKFKRAED YPIDLYYLMD LSYSMKDDLE NVKSLGTDLL NEMRRITSDF
RIGFGSFVEK TVMPYISTTP AKLRNPCTSE QNCTSPFSYK NVLSLTDKGE VFNELVGKQR
ISGNLDSPEG GFDAIMQVAV CGSLIGWRNV TRLLVFSTDA GFHFAGDGKL GGIVLPNDGQ
CHLENDVYTM SHYYDYPSIA HLVQKLSENN IQTIFAVTEE FQPVYKELKN LIPKSAVGTL
SANSSNVIQL IIDAYNSLSS EVILENSKLP EGVTISYKSY CKNGVNGTGE NGRKCSNISI
GDEVQFEISI TANKCPNKNS EIIKIKPLGF TEEVEIILQF ICECECQNEG IPSSPKCHEG
NGSFECGACR CNEGRVGRHC ECSTDEVNSE DMDAYCRKEN SSEICSNNGE CVCGQCVCRK
RDNTNEIYSG KFCECDNFNC DRSNGLICGG NGVCKCRVCE CNPNYTGSAC DCSLDTTSCM
ATNGQICNGR GICECGACKC TDPKFQGPTC EMCQTCLGVC AEHKECVQCR AFNKGEKKDT
CAQECSHFNI TKVENRDKLP QPGQVDPLSH CKEKDVDDCW FYFTYSVNGN NEAIVHVVET
PECPTGPDII PIVAGVVAGI VLIGLALLLI WKLLMIIHDT REFAKFEKEK MNAKWDTGEN
PIYKSAVTTV VNPKYEGK


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