P56199 (ITA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Integrin alpha-1

Alternative name(s):
CD49 antigen-like family member A
Laminin and collagen receptor
VLA-1
CD_antigen=CD49a

Gene names

Name:

ITGA1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1179 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Integrin alpha-1/beta-1 is a receptor for laminin and collagen. It recognizes the proline-hydroxylated sequence G-F-P-G-E-R in collagen.
Subunit structure	Heterodimer of an alpha and a beta subunit. Alpha-1 associates with beta-1. Interacts with RAB21. Ref.5
Subcellular location	Membrane; Single-pass type I membrane protein.
Domain	The integrin I-domain (insert) is a VWFA domain. Integrins with I-domains do not undergo protease cleavage.
Sequence similarities	Belongs to the integrin alpha chain family. Contains 7 FG-GAP repeats. Contains 1 VWFA domain.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Domain	Repeat Signal Transmembrane Transmembrane helix
Ligand	Calcium Magnesium Metal-binding
Molecular function	Integrin Receptor
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	activation of MAPK activity Inferred from electronic annotation. Source: Compara axon guidance Traceable author statement. Source: Reactome cell-matrix adhesion Non-traceable author statement. Source: UniProtKB cellular extravasation Inferred from electronic annotation. Source: Compara integrin-mediated signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW muscle contraction Traceable author statement. Source: Reactome neutrophil chemotaxis Inferred from electronic annotation. Source: Compara positive regulation of neuron apoptotic process Inferred from electronic annotation. Source: Compara vasodilation Inferred from electronic annotation. Source: Compara
Cellular_component	acrosomal vesicle Inferred from electronic annotation. Source: Compara basal part of cell Inferred from electronic annotation. Source: Compara external side of plasma membrane Inferred from electronic annotation. Source: Compara integrin complex Traceable author statement Ref.3. Source: UniProtKB membrane raft Inferred from electronic annotation. Source: Compara neuron projection Inferred from electronic annotation. Source: Compara perikaryon Inferred from electronic annotation. Source: Compara
Molecular_function	collagen binding Traceable author statement Ref.3. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 28

28

Potential

Chain

29 – 1179

1151

Integrin alpha-1

PRO_0000174215

Regions

Topological domain

29 – 1141

1113

Extracellular Potential

Transmembrane

1142 – 1164

23

Helical; Potential

Topological domain

1165 – 1179

15

Cytoplasmic Potential

Repeat

30 – 91

62

FG-GAP 1

Repeat

101 – 160

60

FG-GAP 2

Domain

161 – 360

200

VWFA

Repeat

365 – 417

53

FG-GAP 3

Repeat

422 – 475

54

FG-GAP 4

Repeat

476 – 538

63

FG-GAP 5

Repeat

557 – 615

59

FG-GAP 6

Repeat

619 – 679

61

FG-GAP 7

Calcium binding

498 – 506

9

Potential

Calcium binding

580 – 588

9

Potential

Calcium binding

642 – 650

9

Potential

Motif

1167 – 1171

5

GFFKR motif

Amino acid modifications

Glycosylation

74

1

N-linked (GlcNAc...) Potential

Glycosylation

100

1

N-linked (GlcNAc...) Ref.6

Glycosylation

105

1

N-linked (GlcNAc...) Ref.6

Glycosylation

112

1

N-linked (GlcNAc...) Potential

Glycosylation

217

1

N-linked (GlcNAc...) Ref.6

Glycosylation

317

1

N-linked (GlcNAc...) Potential

Glycosylation

341

1

N-linked (GlcNAc...) Ref.6

Glycosylation

402

1

N-linked (GlcNAc...) Potential

Glycosylation

418

1

N-linked (GlcNAc...) Ref.6

Glycosylation

460

1

N-linked (GlcNAc...) Ref.6

Glycosylation

532

1

N-linked (GlcNAc...) Ref.4 Ref.6

Glycosylation

699

1

N-linked (GlcNAc...) Potential

Glycosylation

748

1

N-linked (GlcNAc...) Potential

Glycosylation

780

1

N-linked (GlcNAc...) Ref.6

Glycosylation

840

1

N-linked (GlcNAc...) Ref.6

Glycosylation

883

1

N-linked (GlcNAc...) Potential

Glycosylation

908

1

N-linked (GlcNAc...) Potential

Glycosylation

915

1

N-linked (GlcNAc...) Potential

Glycosylation

939

1

N-linked (GlcNAc...) Potential

Glycosylation

966

1

N-linked (GlcNAc...) Ref.6

Glycosylation

974

1

N-linked (GlcNAc...) Ref.6

Glycosylation

1008

1

N-linked (GlcNAc...) Ref.6

Glycosylation

1073

1

N-linked (GlcNAc...) Potential

Glycosylation

1083

1

N-linked (GlcNAc...) Potential

Glycosylation

1102

1

N-linked (GlcNAc...) Potential

Glycosylation

1113

1

N-linked (GlcNAc...) Potential

Disulfide bond

82 ↔ 92

By similarity

Disulfide bond

688 ↔ 697

By similarity

Disulfide bond

703 ↔ 756

By similarity

Disulfide bond

808 ↔ 814

By similarity

Disulfide bond

878 ↔ 886

By similarity

Disulfide bond

1030 ↔ 1062

By similarity

Disulfide bond

1065 ↔ 1072

By similarity

Natural variations

Natural variant

480

1

T → M.
Corresponds to variant rs4145748 [ dbSNP | Ensembl ].

VAR_034022

Natural variant

670

1

V → I.
Corresponds to variant rs2279587 [ dbSNP | Ensembl ].

VAR_049630

Natural variant

961

1

I → M.
Corresponds to variant rs12520591 [ dbSNP | Ensembl ].

VAR_034023

Natural variant

1108

1

E → G.
Corresponds to variant rs988574 [ dbSNP | Ensembl ].

VAR_034024

Experimental info

Sequence conflict

198

1

E → K Ref.3

Sequence conflict

254

1

I → T Ref.3

Sequence conflict

705

1

D → E Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

1179

Helix Strand Turn

Details...

Beta strand

171 – 178

8

Helix

186 – 197

12

Beta strand

206 – 222

17

Turn

224 – 226

3

Helix

230 – 238

9

Helix

250 – 259

10

Turn

260 – 262

3

Helix

264 – 266

3

Beta strand

273 – 282

10

Helix

288 – 299

12

Beta strand

302 – 309

8

Helix

311 – 315

5

Helix

321 – 330

10

Helix

335 – 338

4

Beta strand

339 – 344

6

Helix

345 – 351

7

Helix

352 – 359

8

Helix

1143 – 1168

26

Sequences

	Sequence		Length	Mass (Da)
	P56199 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 1A86F30FD916C845	FASTA	1,179	130,848
	10 20 30 40 50 60 MAPRPRARPG VAVACCWLLT VVLRCCVSFN VDVKNSMTFS GPVEDMFGYT VQQYENEEGK 70 80 90 100 110 120 WVLIGSPLVG QPKNRTGDVY KCPVGRGESL PCVKLDLPVN TSIPNVTEVK ENMTFGSTLV 130 140 150 160 170 180 TNPNGGFLAC GPLYAYRCGH LHYTTGICSD VSPTFQVVNS IAPVQECSTQ LDIVIVLDGS 190 200 210 220 230 240 NSIYPWDSVT AFLNDLLERM DIGPKQTQVG IVQYGENVTH EFNLNKYSST EEVLVAAKKI 250 260 270 280 290 300 VQRGGRQTMT ALGIDTARKE AFTEARGARR GVKKVMVIVT DGESHDNHRL KKVIQDCEDE 310 320 330 340 350 360 NIQRFSIAIL GSYNRGNLST EKFVEEIKSI ASEPTEKHFF NVSDELALVT IVKTLGERIF 370 380 390 400 410 420 ALEATADQSA ASFEMEMSQT GFSAHYSQDW VMLGAVGAYD WNGTVVMQKA SQIIIPRNTT 430 440 450 460 470 480 FNVESTKKNE PLASYLGYTV NSATASSGDV LYIAGQPRYN HTGQVIIYRM EDGNIKILQT 490 500 510 520 530 540 LSGEQIGSYF GSILTTTDID KDSNTDILLV GAPMYMGTEK EEQGKVYVYA LNQTRFEYQM 550 560 570 580 590 600 SLEPIKQTCC SSRQHNSCTT ENKNEPCGAR FGTAIAAVKD LNLDGFNDIV IGAPLEDDHG 610 620 630 640 650 660 GAVYIYHGSG KTIRKEYAQR IPSGGDGKTL KFFGQSIHGE MDLNGDGLTD VTIGGLGGAA 670 680 690 700 710 720 LFWSRDVAVV KVTMNFEPNK VNIQKKNCHM EGKETVCINA TVCFDVKLKS KEDTIYEADL 730 740 750 760 770 780 QYRVTLDSLR QISRSFFSGT QERKVQRNIT VRKSECTKHS FYMLDKHDFQ DSVRITLDFN 790 800 810 820 830 840 LTDPENGPVL DDSLPNSVHE YIPFAKDCGN KEKCISDLSL HVATTEKDLL IVRSQNDKFN 850 860 870 880 890 900 VSLTVKNTKD SAYNTRTIVH YSPNLVFSGI EAIQKDSCES NHNITCKVGY PFLRRGEMVT 910 920 930 940 950 960 FKILFQFNTS YLMENVTIYL SATSDSEEPP ETLSDNVVNI SIPVKYEVGL QFYSSASEYH 970 980 990 1000 1010 1020 ISIAANETVP EVINSTEDIG NEINIFYLIR KSGSFPMPEL KLSISFPNMT SNGYPVLYPT 1030 1040 1050 1060 1070 1080 GLSSSENANC RPHIFEDPFS INSGKKMTTS TDHLKRGTIL DCNTCKFATI TCNLTSSDIS 1090 1100 1110 1120 1130 1140 QVNVSLILWK PTFIKSYFSS LNLTIRGELR SENASLVLSS SNQKRELAIQ ISKDGLPGRV 1150 1160 1170 PLWVILLSAF AGLLLLMLLI LALWKIGFFK RPLKKKMEK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The DNA sequence and comparative analysis of human chromosome 5." Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M. Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[3]	"Expression of native and truncated forms of the human integrin alpha 1 subunit." Briesewitz R., Epstein M.R., Marcantonio E.E. J. Biol. Chem. 268:2989-2996(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 29-1179.
[4]	"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry." Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D. J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-532, MASS SPECTROMETRY. Tissue: Plasma.
[5]	"Small GTPase Rab21 regulates cell adhesion and controls endosomal traffic of beta1-integrins." Pellinen T., Arjonen A., Vuoriluoto K., Kallio K., Fransen J.A.M., Ivaska J. J. Cell Biol. 173:767-780(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RAB21.
[6]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-100; ASN-105; ASN-217; ASN-341; ASN-418; ASN-460; ASN-532; ASN-780; ASN-840; ASN-966; ASN-974 AND ASN-1008, MASS SPECTROMETRY. Tissue: Liver.
[7]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]	"Trench-shaped binding sites promote multiple classes of interactions between collagen and the adherence receptors, alpha(1)beta(1) integrin and Staphylococcus aureus cna MSCRAMM." Rich R.L., Deivanayagam C.C., Owens R.T., Carson M., Hook A., Moore D., Symersky J., Yang V.W., Narayana S.V., Hook M. J. Biol. Chem. 274:24906-24913(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 168-359.
[9]	"Jararhagin-derived RKKH peptides induce structural changes in alpha1I domain of human integrin alpha1beta1." Nymalm Y., Puranen J.S., Nyholm T.K., Kapyla J., Kidron H., Pentikainen O.T., Airenne T.T., Heino J., Slotte J.P., Johnson M.S., Salminen T.A. J. Biol. Chem. 279:7962-7970(2004) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.87 ANGSTROMS) OF 166-356.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AC027326 Genomic DNA. No translation available.
AC022133 Genomic DNA. No translation available.
AC025180 Genomic DNA. No translation available.
BC137121 mRNA. Translation: AAI37122.1.
BC137122 mRNA. Translation: AAI37123.1.
X68742 mRNA. No translation available.

IPI

IPI00743104.

PIR

A45226.

RefSeq

NP_852478.1. NM_181501.1.

UniGene

Hs.644352.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1PT6	X-ray	1.87	A/B	166-366	[»]
1QC5	X-ray	2.00	A/B	168-359	[»]
1QCY	X-ray	2.30	A	169-361	[»]
2L8S	NMR	-	A	1135-1179	[»]
4A0Q	X-ray	1.90	A/B	168-366	[»]

ProteinModelPortal

P56199.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-206N.

IntAct

P56199. 5 interactions.

STRING

9606.ENSP00000282588.

PTM databases

PhosphoSite

P56199.

Polymorphism databases

DMDM

124056463.

Proteomic databases

PaxDb

P56199.

PRIDE

P56199.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000282588; ENSP00000282588; ENSG00000213949.

GeneID

3672.

KEGG

hsa:3672.

UCSC

uc003jou.3. human.

Organism-specific databases

CTD

3672.

GeneCards

GC05P052083.

HGNC

HGNC:6134. ITGA1.

HPA

HPA042555.

MIM

192968. gene.

neXtProt

NX_P56199.

PharmGKB

PA29935.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG322251.

HOGENOM

HOG000059610.

HOVERGEN

HBG006185.

InParanoid

P56199.

KO

K06480.

OMA

MDIGPKQ.

OrthoDB

EOG4THVS7.

PhylomeDB

P56199.

Enzyme and pathway databases

Pathway_Interaction_DB

arf6_traffickingpathway. Arf6 trafficking events.
prlsignalingeventspathway. Signaling events mediated by PRL.
lymphangiogenesis_pathway. VEGFR3 signaling in lymphatic endothelium.

Reactome

REACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_17044. Muscle contraction.

Gene expression databases

Bgee

P56199.

Genevestigator

P56199.

GermOnline

ENSG00000152684. Homo sapiens.

Family and domain databases

InterPro

IPR013517. FG-GAP.
IPR013519. Int_alpha_beta-p.
IPR000413. Integrin_alpha.
IPR013649. Integrin_alpha-2.
IPR018184. Integrin_alpha_C_CS.
IPR002035. VWF_A.
[Graphical view]

Pfam

PF01839. FG-GAP. 1 hit.
PF08441. Integrin_alpha2. 1 hit.
PF00092. VWA. 1 hit.
[Graphical view]

PRINTS

PR01185. INTEGRINA.

SMART

SM00191. Int_alpha. 5 hits.
SM00327. VWA. 1 hit.
[Graphical view]

PROSITE

PS51470. FG_GAP. 7 hits.
PS00242. INTEGRIN_ALPHA. 1 hit.
PS50234. VWFA. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P56199.

ChEMBL

CHEMBL3682.

EvolutionaryTrace

P56199.

GenomeRNAi

3672.

NextBio

14373.

SOURCE

Search...

Entry information

Entry name

ITA1_HUMAN

Accession

Primary (citable) accession number: P56199
Secondary accession number(s): B2RNU0

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 135 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.