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.
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	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.2 Traceable author statement. Source: UniProtKB
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW collagen binding Ref.2 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...) Potential

Glycosylation

105

1

N-linked (GlcNAc...) Potential

Glycosylation

112

1

N-linked (GlcNAc...) Potential

Glycosylation

217

1

N-linked (GlcNAc...) Potential

Glycosylation

317

1

N-linked (GlcNAc...) Potential

Glycosylation

341

1

N-linked (GlcNAc...) Potential

Glycosylation

402

1

N-linked (GlcNAc...) Potential

Glycosylation

418

1

N-linked (GlcNAc...) Potential

Glycosylation

460

1

N-linked (GlcNAc...) Potential

Glycosylation

532

1

N-linked (GlcNAc...)

Glycosylation

699

1

N-linked (GlcNAc...) Potential

Glycosylation

748

1

N-linked (GlcNAc...) Potential

Glycosylation

780

1

N-linked (GlcNAc...) Potential

Glycosylation

840

1

N-linked (GlcNAc...) Potential

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...) Potential

Glycosylation

974

1

N-linked (GlcNAc...) Potential

Glycosylation

1008

1

N-linked (GlcNAc...) Potential

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

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.2

Sequence conflict

254

1

I → T Ref.2

Sequence conflict

705

1

D → E Ref.2

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]	"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.
[3]	"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.
[4]	"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.
[5]	"Jararhagin-derived RKKH peptides induce structural changes in alpha1I domain of human integrin alpha1beta1." Nymalm Y., Puranen J.S., Nyholm T.K., K