Reviewed, UniProtKB/Swiss-Prot P56199 (ITA1_HUMAN)

Names and origin

Protein names

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

Gene names

Name:

ITGA1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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
Ligand	Calcium Magnesium
Molecular function	Integrin Receptor
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	cell-matrix adhesion Non-traceable author statement. Source: UniProtKB integrin-mediated signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integrin complex Ref.3 Traceable author statement. Source: UniProtKB
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW collagen binding Ref.3 Traceable author statement. Source: UniProtKB magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW receptor activity 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

Potential

Topological domain

1165 – 1179

15

Cytoplasmic Potential

Repeat

44 – 103

60

FG-GAP 1

Repeat

104 – ?

FG-GAP 2

Domain

147 – 360

214

VWFA

Repeat

349 – 404

56

FG-GAP 3

Repeat

405 – 457

53

FG-GAP 4

Repeat

459 – 520

62

FG-GAP 5

Repeat

540 – 599

60

FG-GAP 6

Repeat

602 – 654

53

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...)

Glycosylation

105

1

N-linked (GlcNAc...)

Glycosylation

112

1

N-linked (GlcNAc...) Potential

Glycosylation

217

1

N-linked (GlcNAc...)

Glycosylation

317

1

N-linked (GlcNAc...) Potential

Glycosylation

341

1

N-linked (GlcNAc...)

Glycosylation

402

1

N-linked (GlcNAc...) Potential

Glycosylation

418

1

N-linked (GlcNAc...)

Glycosylation

460

1

N-linked (GlcNAc...)

Glycosylation

532

1

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

Glycosylation

699

1

N-linked (GlcNAc...) Potential

Glycosylation

748

1

N-linked (GlcNAc...) Potential

Glycosylation

780

1

N-linked (GlcNAc...)

Glycosylation

840

1

N-linked (GlcNAc...)

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...)

Glycosylation

974

1

N-linked (GlcNAc...)

Glycosylation

1008

1

N-linked (GlcNAc...)

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: dbSNP rs4145748.

VAR_034022

Natural variant

670

1

V → I: dbSNP rs2279587.

VAR_049630

Natural variant

961

1

I → M: dbSNP rs12520591.

VAR_034023

Natural variant

1108

1

E → G: dbSNP rs988574.

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

Sequences

	Sequence		Length	Mass (Da)
	P56199-1 [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: 15372022] [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: 15489334] [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: 8428973] [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: 16335952] [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: 16754960] [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: 19159218] [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]	"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: 10455165] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 168-359.
[8]	"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: 14660600] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.87 ANGSTROMS) OF 166-356.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.

UniGene

Hs.644352

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1PT6	X-ray	1.87	A/B	166-366	[»]
1QC5	X-ray	2.00	A	168-359	[»]
			B	168-359	[»]
1QCY	X-ray	2.30	A	169-361	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:206N.

PTM databases

PhosphoSite

P56199.

2-D gel databases

Cornea-2DPAGE

P56199.

Proteomic databases

PRIDE

P56199.

Genome annotation databases

Ensembl

ENSG00000213949. Homo sapiens. [Contig view]

GeneID

3672.

KEGG

hsa:3672.

Organism-specific databases

GeneCards

GC05P052119.

H-InvDB

HIX0004852.

HGNC

HGNC:6134. ITGA1.

MIM

192968. gene.

PharmGKB

PA29935.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

P56199.

OMA

P56199. EYQMSLE.

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_13552. Integrin cell surface interactions.

Gene expression databases

ArrayExpress

P56199.

Bgee

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. 2 hits.
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

PS00242. INTEGRIN_ALPHA. 1 hit.
PS50234. VWFA. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

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:	June 16, 2009
This is version 96 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)