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P07228 (ITB1_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Integrin beta-1
Alternative name(s):
CSAT antigen
JG22 antigen
RGD-receptor
Gene names
Name:ITGB1
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

Protein attributes

Sequence length803 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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-1 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. 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. May be involved in up-regulation of the activity of kinases such as PKC via binding to KRT1. Together with KRT1 and GNB2L1, serves as a platform for SRC activation or inactivation By similarity.

Subunit structure

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 By similarity.

Subcellular location

Cell membrane; Single-pass type I membrane protein By similarity. Melanosome By similarity.

Tissue specificity

Expressed on surface of embryonic fibroblasts (at protein level). Ref.1

Post-translational modification

The cysteine residues are involved in intrachain disulfide bonds.

Sequence similarities

Belongs to the integrin beta chain family.

Contains 1 VWFA domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ACTN1P050944EBI-5606437,EBI-5847257
FLNAP213332EBI-5606437,EBI-350432From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 By similarity
Chain25 – 803779Integrin beta-1
PRO_0000016337

Regions

Topological domain25 – 733709Extracellular Potential
Transmembrane734 – 75623Helical; Potential
Topological domain757 – 80347Cytoplasmic Potential
Domain144 – 382239VWFA
Repeat471 – 52050I
Repeat521 – 56444II
Repeat565 – 60339III
Repeat604 – 64037IV
Region471 – 640170Cysteine-rich tandem repeats

Sites

Metal binding1561Magnesium By similarity
Metal binding1581Calcium 1; via carbonyl oxygen By similarity
Metal binding1601Calcium 1 By similarity
Metal binding1611Calcium 1 By similarity
Metal binding1931Calcium 2 By similarity
Metal binding2481Calcium 2 By similarity
Metal binding2501Calcium 2 By similarity
Metal binding2521Calcium 2; via carbonyl oxygen By similarity
Metal binding2531Calcium 2 By similarity
Metal binding2531Magnesium By similarity

Amino acid modifications

Modified residue251Blocked amino end (Gln)
Modified residue7881Phosphotyrosine; by Tyr-kinases Potential
Glycosylation2161N-linked (GlcNAc...) Potential
Glycosylation2731N-linked (GlcNAc...) Potential
Glycosylation3671N-linked (GlcNAc...) Potential
Glycosylation4101N-linked (GlcNAc...) Potential
Glycosylation4211N-linked (GlcNAc...) Potential
Glycosylation4331N-linked (GlcNAc...) Potential
Glycosylation4451N-linked (GlcNAc...) Potential
Glycosylation4861N-linked (GlcNAc...) Potential
Glycosylation5251N-linked (GlcNAc...) Potential
Glycosylation5891N-linked (GlcNAc...) Potential
Glycosylation6241N-linked (GlcNAc...) Potential
Glycosylation6741N-linked (GlcNAc...) Potential
Disulfide bond31 ↔ 49 By similarity
Disulfide bond39 ↔ 469 By similarity
Disulfide bond42 ↔ 79 By similarity
Disulfide bond52 ↔ 68 By similarity
Disulfide bond211 ↔ 217 By similarity
Disulfide bond265 ↔ 305 By similarity
Disulfide bond405 ↔ 419 By similarity
Disulfide bond439 ↔ 467 By similarity
Disulfide bond471 ↔ 696 By similarity
Disulfide bond482 ↔ 494 By similarity
Disulfide bond491 ↔ 530 By similarity
Disulfide bond496 ↔ 505 By similarity
Disulfide bond507 ↔ 521 By similarity
Disulfide bond536 ↔ 541 By similarity
Disulfide bond538 ↔ 573 By similarity
Disulfide bond543 ↔ 558 By similarity
Disulfide bond560 ↔ 565 By similarity
Disulfide bond579 ↔ 584 By similarity
Disulfide bond581 ↔ 612 By similarity
Disulfide bond586 ↔ 595 By similarity
Disulfide bond597 ↔ 604 By similarity
Disulfide bond618 ↔ 623 By similarity
Disulfide bond620 ↔ 666 By similarity
Disulfide bond625 ↔ 635 By similarity
Disulfide bond638 ↔ 641 By similarity
Disulfide bond645 ↔ 654 By similarity
Disulfide bond651 ↔ 728 By similarity
Disulfide bond670 ↔ 704 By similarity

Sequences

Sequence LengthMass (Da)Tools
P07228 [UniParc].

Last modified April 1, 1988. Version 1.
Checksum: 2F6FEFCDF2C80457

FASTA80388,554
        10         20         30         40         50         60 
MAETNLTLLT WAGILCCLIW SGSAQQGGSD CIKANAKSCG ECIQAGPNCG WCKKTDFLQE 

        70         80         90        100        110        120 
GEPTSARCDD LAALKSKGCP EQDIENPRGS KRVLEDREVT NRKIGAAEKL KPEAITQIQP 

       130        140        150        160        170        180 
QKLVLQLRVG EPQTFSLKFK RAEDYPIDLY YLMDLSYSMK DDLENVKSLG TALMREMEKI 

       190        200        210        220        230        240 
TSDFRIGFGS FVEKTVMPYI STTPAKLRNP CTGDQNCTSP FSYKNVLSLT SEGNKFNELV 

       250        260        270        280        290        300 
GKQHISGNLD SPEGGFDAIM QVAVCGDQIG WRNVTRLLVF STDAGFHFAG DGKLGGIVLP 

       310        320        330        340        350        360 
NDGKCHLENN MYTMSHYYDY PSIAHLVQKL SENNIQTIFA VTEEFQAVYK ELKNLIPKSA 

       370        380        390        400        410        420 
VGTLSSNSSN VIQLIIDAYN SLSSEVILEN SKLPKEVTIS YKSYCKNGVN DTQEDGRKCS 

       430        440        450        460        470        480 
NISIGDEVRF EINVTANECP KKGQNETIKI KPLGFTEEVE IHLQFICDCL CQSEGEPNSP 

       490        500        510        520        530        540 
ACHDGNGTFE CGACRCNEGR IGRLCECSTD EVNSEDMDAY CRRENSTEIC SNNGECICGQ 

       550        560        570        580        590        600 
CVCKKRENTN EVYSGKYCEC DNFNCDRSNG LICGGNGICK CRVCECFPNF TGSACDCSLD 

       610        620        630        640        650        660 
TTPCMAGNGQ ICNGRGTCEC GTCNCTDPKF QGPTCEMCQT CLGVCAEHKD CVQCRAFEKG 

       670        680        690        700        710        720 
EKKETCSQEC MHFNMTRVES RGKLPQPVHP DPLSHCKEKD VGDCWFYFTY SVNSNGEASV 

       730        740        750        760        770        780 
HVVETPECPS GPDIIPIVAG VVAGIVLIGL ALLLIWKLLM IIHDRREFAK FEKEKMNAKW 

       790        800 
DTGENPIYKS AVTTVVNPKY EGK

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References

[1]"Structure of integrin, a glycoprotein involved in the transmembrane linkage between fibronectin and actin."
Tamkun J.W., Desimone D.W., Fonda D., Patel R.S., Buck C., Horwitz A.F., Hynes R.O.
Cell 46:271-282(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M14049 mRNA. Translation: AAA48926.1.
IPIIPI00735136.
PIRIJCH3. A23947.
UniGeneGga.111.

3D structure databases

ProteinModelPortalP07228.
SMRP07228. Positions 726-802.
ModBaseSearch...

Protein-protein interaction databases

IntActP07228. 3 interactions.
STRING9031.ENSGALP00000011559.

Proteomic databases

PaxDbP07228.
PRIDEP07228.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGNOG287997.
HOGENOMHOG000252936.
HOVERGENHBG006190.
InParanoidP07228.
OrthoDBEOG4K9BBM.

Family and domain databases

Gene3D1.20.5.630. 1 hit.
InterProIPR013111. EGF_extracell.
IPR027071. Integrin_beta-1.
IPR015812. Integrin_bsu.
IPR014836. Integrin_bsu_cyt_dom.
IPR002369. Integrin_bsu_N.
IPR012896. Integrin_bsu_tail.
IPR003659. Plexin-like.
IPR016201. Plexin-like_fold.
IPR002035. VWF_A.
[Graphical view]
PANTHERPTHR10082. PTHR10082. 1 hit.
PTHR10082:SF28. PTHR10082:SF28. 1 hit.
PfamPF07974. EGF_2. 1 hit.
PF08725. Integrin_b_cyt. 1 hit.
PF07965. Integrin_B_tail. 1 hit.
PF00362. Integrin_beta. 1 hit.
[Graphical view]
PIRSFPIRSF002512. Integrin_B. 1 hit.
PRINTSPR01186. INTEGRINB.
SMARTSM00187. INB. 1 hit.
SM00423. PSI. 1 hit.
SM00327. VWA. 1 hit.
[Graphical view]
SUPFAMSSF69687. Integrin_bsu_tail. 1 hit.
SSF103575. Plexin-like_fold. 1 hit.
PROSITEPS00022. EGF_1. 2 hits. Uncertain.
PS00243. INTEGRIN_BETA. 3 hits.
PS50234. VWFA. False negative.
[Graphical view]
ProtoNetSearch...

Other

NextBio20813580.

Entry information

Entry nameITB1_CHICK
AccessionPrimary (citable) accession number: P07228
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: May 1, 2013
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents