ITA1_HUMAN
ID ITA1_HUMAN Reviewed; 1179 AA.
AC P56199; B2RNU0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=Integrin alpha-1;
DE AltName: Full=CD49 antigen-like family member A;
DE AltName: Full=Laminin and collagen receptor;
DE AltName: Full=VLA-1;
DE AltName: CD_antigen=CD49a;
DE Flags: Precursor;
GN Name=ITGA1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 29-1179.
RX PubMed=8428973; DOI=10.1016/s0021-9258(18)53871-0;
RA Briesewitz R., Epstein M.R., Marcantonio E.E.;
RT "Expression of native and truncated forms of the human integrin alpha 1
RT subunit.";
RL J. Biol. Chem. 268:2989-2996(1993).
RN [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-532.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [5]
RP FUNCTION IN EGFR SIGNALING, AND INTERACTION WITH PTPN2.
RX PubMed=15592458; DOI=10.1038/ncb1209;
RA Mattila E., Pellinen T., Nevo J., Vuoriluoto K., Arjonen A., Ivaska J.;
RT "Negative regulation of EGFR signalling through integrin-alpha1beta1-
RT mediated activation of protein tyrosine phosphatase TCPTP.";
RL Nat. Cell Biol. 7:78-85(2005).
RN [6]
RP INTERACTION WITH RAB21.
RX PubMed=16754960; DOI=10.1083/jcb.200509019;
RA Pellinen T., Arjonen A., Vuoriluoto K., Kallio K., Fransen J.A.M.,
RA Ivaska J.;
RT "Small GTPase Rab21 regulates cell adhesion and controls endosomal traffic
RT of beta1-integrins.";
RL J. Cell Biol. 173:767-780(2006).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-100; ASN-105; ASN-217; ASN-341;
RP ASN-418; ASN-460; ASN-532; ASN-780; ASN-840; ASN-966; ASN-974 AND ASN-1008.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 168-359.
RX PubMed=10455165; DOI=10.1074/jbc.274.35.24906;
RA Rich R.L., Deivanayagam C.C., Owens R.T., Carson M., Hook A., Moore D.,
RA Symersky J., Yang V.W., Narayana S.V., Hook M.;
RT "Trench-shaped binding sites promote multiple classes of interactions
RT between collagen and the adherence receptors, alpha(1)beta(1) integrin and
RT Staphylococcus aureus cna MSCRAMM.";
RL J. Biol. Chem. 274:24906-24913(1999).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.87 ANGSTROMS) OF 166-356.
RX PubMed=14660600; DOI=10.1074/jbc.m312912200;
RA Nymalm Y., Puranen J.S., Nyholm T.K., Kapyla J., Kidron H.,
RA Pentikainen O.T., Airenne T.T., Heino J., Slotte J.P., Johnson M.S.,
RA Salminen T.A.;
RT "Jararhagin-derived RKKH peptides induce structural changes in alpha1I
RT domain of human integrin alpha1beta1.";
RL J. Biol. Chem. 279:7962-7970(2004).
CC -!- FUNCTION: Integrin alpha-1/beta-1 is a receptor for laminin and
CC collagen. It recognizes the proline-hydroxylated sequence G-F-P-G-E-R
CC in collagen. Involved in anchorage-dependent, negative regulation of
CC EGF-stimulated cell growth. {ECO:0000269|PubMed:15592458}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Alpha-1 associates
CC with beta-1. Interacts with RAB21. Interacts (via cytoplasmic domain)
CC with PTPN2; activates PTPN2 phosphatase activity towards EGFR and
CC negatively regulates EGF signaling. {ECO:0000269|PubMed:15592458,
CC ECO:0000269|PubMed:16754960}.
CC -!- INTERACTION:
CC P56199; P04512; Xeno; NbExp=2; IntAct=EBI-2554465, EBI-15711650;
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- DOMAIN: The integrin I-domain (insert) is a VWFA domain. Integrins with
CC I-domains do not undergo protease cleavage.
CC -!- SIMILARITY: Belongs to the integrin alpha chain family. {ECO:0000305}.
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DR EMBL; AC027326; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC022133; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC025180; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC137121; AAI37122.1; -; mRNA.
DR EMBL; BC137122; AAI37123.1; -; mRNA.
DR EMBL; X68742; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS3955.1; -.
DR PIR; A45226; A45226.
DR RefSeq; NP_852478.1; NM_181501.1.
DR PDB; 1PT6; X-ray; 1.87 A; A/B=166-366.
DR PDB; 1QC5; X-ray; 2.00 A; A/B=168-359.
DR PDB; 1QCY; X-ray; 2.30 A; A=169-361.
DR PDB; 2L8S; NMR; -; A=1135-1179.
DR PDB; 2M32; NMR; -; A=168-359.
DR PDB; 4A0Q; X-ray; 1.90 A; A/B=166-366.
DR PDB; 5HGJ; X-ray; 1.40 A; A/B=170-364.
DR PDBsum; 1PT6; -.
DR PDBsum; 1QC5; -.
DR PDBsum; 1QCY; -.
DR PDBsum; 2L8S; -.
DR PDBsum; 2M32; -.
DR PDBsum; 4A0Q; -.
DR PDBsum; 5HGJ; -.
DR AlphaFoldDB; P56199; -.
DR BMRB; P56199; -.
DR SMR; P56199; -.
DR BioGRID; 109879; 44.
DR ComplexPortal; CPX-1798; Integrin alpha1-beta1 complex.
DR CORUM; P56199; -.
DR DIP; DIP-206N; -.
DR IntAct; P56199; 21.
DR MINT; P56199; -.
DR STRING; 9606.ENSP00000282588; -.
DR BindingDB; P56199; -.
DR ChEMBL; CHEMBL3682; -.
DR GuidetoPHARMACOLOGY; 2437; -.
DR TCDB; 8.A.54.1.1; the integrin (integrin) family.
DR GlyConnect; 1405; 8 N-Linked glycans (4 sites).
DR GlyGen; P56199; 26 sites, 7 N-linked glycans (4 sites).
DR iPTMnet; P56199; -.
DR PhosphoSitePlus; P56199; -.
DR BioMuta; ITGA1; -.
DR DMDM; 124056463; -.
DR CPTAC; CPTAC-1614; -.
DR EPD; P56199; -.
DR jPOST; P56199; -.
DR MassIVE; P56199; -.
DR MaxQB; P56199; -.
DR PaxDb; P56199; -.
DR PeptideAtlas; P56199; -.
DR PRIDE; P56199; -.
DR ProteomicsDB; 56903; -.
DR ABCD; P56199; 9 sequenced antibodies.
DR Antibodypedia; 10955; 577 antibodies from 38 providers.
DR DNASU; 3672; -.
DR Ensembl; ENST00000282588.7; ENSP00000282588.5; ENSG00000213949.10.
DR GeneID; 3672; -.
DR KEGG; hsa:3672; -.
DR MANE-Select; ENST00000282588.7; ENSP00000282588.5; NM_181501.2; NP_852478.1.
DR UCSC; uc003jou.4; human.
DR CTD; 3672; -.
DR DisGeNET; 3672; -.
DR GeneCards; ITGA1; -.
DR HGNC; HGNC:6134; ITGA1.
DR HPA; ENSG00000213949; Low tissue specificity.
DR MIM; 192968; gene.
DR neXtProt; NX_P56199; -.
DR OpenTargets; ENSG00000213949; -.
DR PharmGKB; PA29935; -.
DR VEuPathDB; HostDB:ENSG00000213949; -.
DR eggNOG; KOG3637; Eukaryota.
DR GeneTree; ENSGT00940000157646; -.
DR HOGENOM; CLU_004111_2_1_1; -.
DR InParanoid; P56199; -.
DR OMA; THTFLAI; -.
DR OrthoDB; 66046at2759; -.
DR PhylomeDB; P56199; -.
DR TreeFam; TF105391; -.
DR PathwayCommons; P56199; -.
DR Reactome; R-HSA-216083; Integrin cell surface interactions.
DR Reactome; R-HSA-3000157; Laminin interactions.
DR Reactome; R-HSA-416700; Other semaphorin interactions.
DR Reactome; R-HSA-445355; Smooth Muscle Contraction.
DR Reactome; R-HSA-447041; CHL1 interactions.
DR Reactome; R-HSA-75892; Platelet Adhesion to exposed collagen.
DR SignaLink; P56199; -.
DR SIGNOR; P56199; -.
DR BioGRID-ORCS; 3672; 15 hits in 1066 CRISPR screens.
DR ChiTaRS; ITGA1; human.
DR EvolutionaryTrace; P56199; -.
DR GeneWiki; CD49a; -.
DR GenomeRNAi; 3672; -.
DR Pharos; P56199; Tbio.
DR PRO; PR:P56199; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; P56199; protein.
DR Bgee; ENSG00000213949; Expressed in calcaneal tendon and 182 other tissues.
DR ExpressionAtlas; P56199; baseline and differential.
DR Genevisible; P56199; HS.
DR GO; GO:0001669; C:acrosomal vesicle; IEA:Ensembl.
DR GO; GO:0045178; C:basal part of cell; IEA:Ensembl.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
DR GO; GO:0034665; C:integrin alpha1-beta1 complex; IDA:UniProtKB.
DR GO; GO:0008305; C:integrin complex; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0045121; C:membrane raft; IEA:Ensembl.
DR GO; GO:0043005; C:neuron projection; IEA:Ensembl.
DR GO; GO:0043204; C:perikaryon; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005518; F:collagen binding; TAS:UniProtKB.
DR GO; GO:0098639; F:collagen binding involved in cell-matrix adhesion; IMP:UniProtKB.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019903; F:protein phosphatase binding; IPI:UniProtKB.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0007160; P:cell-matrix adhesion; IMP:UniProtKB.
DR GO; GO:0045123; P:cellular extravasation; IEA:Ensembl.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0048812; P:neuron projection morphogenesis; IEA:Ensembl.
DR GO; GO:0030593; P:neutrophil chemotaxis; IEA:Ensembl.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IEA:Ensembl.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0032516; P:positive regulation of phosphoprotein phosphatase activity; IDA:UniProtKB.
DR GO; GO:0042311; P:vasodilation; IEA:Ensembl.
DR Gene3D; 2.130.10.130; -; 1.
DR Gene3D; 3.40.50.410; -; 1.
DR InterPro; IPR013517; FG-GAP.
DR InterPro; IPR013519; Int_alpha_beta-p.
DR InterPro; IPR000413; Integrin_alpha.
DR InterPro; IPR013649; Integrin_alpha-2.
DR InterPro; IPR018184; Integrin_alpha_C_CS.
DR InterPro; IPR028994; Integrin_alpha_N.
DR InterPro; IPR032695; Integrin_dom_sf.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR Pfam; PF01839; FG-GAP; 2.
DR Pfam; PF08441; Integrin_alpha2; 1.
DR Pfam; PF00092; VWA; 1.
DR PRINTS; PR01185; INTEGRINA.
DR SMART; SM00191; Int_alpha; 5.
DR SMART; SM00327; VWA; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR SUPFAM; SSF69179; SSF69179; 3.
DR SUPFAM; SSF69318; SSF69318; 1.
DR PROSITE; PS51470; FG_GAP; 7.
DR PROSITE; PS00242; INTEGRIN_ALPHA; 1.
DR PROSITE; PS50234; VWFA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cell adhesion; Disulfide bond; Glycoprotein;
KW Integrin; Magnesium; Membrane; Metal-binding; Receptor; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..1179
FT /note="Integrin alpha-1"
FT /id="PRO_0000174215"
FT TOPO_DOM 29..1141
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1142..1164
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1165..1179
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 30..91
FT /note="FG-GAP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 101..160
FT /note="FG-GAP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT DOMAIN 161..360
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT REPEAT 365..417
FT /note="FG-GAP 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 422..475
FT /note="FG-GAP 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 476..538
FT /note="FG-GAP 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 557..615
FT /note="FG-GAP 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 619..679
FT /note="FG-GAP 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT MOTIF 1167..1171
FT /note="GFFKR motif"
FT BINDING 498
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 500
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 502
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 506
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 580
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 582
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 584
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 588
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 642
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 644
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 646
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 650
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 317
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 341
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 402
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 418
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 460
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 532
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19159218"
FT CARBOHYD 699
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 748
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 780
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 840
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 883
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 908
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 915
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 939
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 966
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 974
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 1008
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 1073
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1083
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 82..92
FT /evidence="ECO:0000250"
FT DISULFID 688..697
FT /evidence="ECO:0000250"
FT DISULFID 703..756
FT /evidence="ECO:0000250"
FT DISULFID 808..814
FT /evidence="ECO:0000250"
FT DISULFID 878..886
FT /evidence="ECO:0000250"
FT DISULFID 1030..1062
FT /evidence="ECO:0000250"
FT DISULFID 1065..1072
FT /evidence="ECO:0000250"
FT VARIANT 480
FT /note="T -> M (in dbSNP:rs4145748)"
FT /id="VAR_034022"
FT VARIANT 670
FT /note="V -> I (in dbSNP:rs2279587)"
FT /id="VAR_049630"
FT VARIANT 961
FT /note="I -> M (in dbSNP:rs12520591)"
FT /id="VAR_034023"
FT VARIANT 1108
FT /note="E -> G (in dbSNP:rs988574)"
FT /id="VAR_034024"
FT CONFLICT 198
FT /note="E -> K (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 254
FT /note="I -> T (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 705
FT /note="D -> E (in Ref. 3)"
FT /evidence="ECO:0000305"
FT STRAND 171..178
FT /evidence="ECO:0007829|PDB:5HGJ"
FT HELIX 187..197
FT /evidence="ECO:0007829|PDB:5HGJ"
FT STRAND 206..222
FT /evidence="ECO:0007829|PDB:5HGJ"
FT TURN 224..226
FT /evidence="ECO:0007829|PDB:1PT6"
FT HELIX 230..238
FT /evidence="ECO:0007829|PDB:5HGJ"
FT HELIX 250..259
FT /evidence="ECO:0007829|PDB:5HGJ"
FT TURN 260..262
FT /evidence="ECO:0007829|PDB:5HGJ"
FT HELIX 264..266
FT /evidence="ECO:0007829|PDB:5HGJ"
FT STRAND 272..282
FT /evidence="ECO:0007829|PDB:5HGJ"
FT HELIX 287..289
FT /evidence="ECO:0007829|PDB:5HGJ"
FT HELIX 290..299
FT /evidence="ECO:0007829|PDB:5HGJ"
FT STRAND 302..309
FT /evidence="ECO:0007829|PDB:5HGJ"
FT HELIX 311..315
FT /evidence="ECO:0007829|PDB:5HGJ"
FT HELIX 321..330
FT /evidence="ECO:0007829|PDB:5HGJ"
FT HELIX 335..338
FT /evidence="ECO:0007829|PDB:5HGJ"
FT STRAND 339..344
FT /evidence="ECO:0007829|PDB:5HGJ"
FT HELIX 345..351
FT /evidence="ECO:0007829|PDB:5HGJ"
FT HELIX 352..359
FT /evidence="ECO:0007829|PDB:5HGJ"
FT HELIX 1143..1168
FT /evidence="ECO:0007829|PDB:2L8S"
SQ SEQUENCE 1179 AA; 130848 MW; 1A86F30FD916C845 CRC64;
MAPRPRARPG VAVACCWLLT VVLRCCVSFN VDVKNSMTFS GPVEDMFGYT VQQYENEEGK
WVLIGSPLVG QPKNRTGDVY KCPVGRGESL PCVKLDLPVN TSIPNVTEVK ENMTFGSTLV
TNPNGGFLAC GPLYAYRCGH LHYTTGICSD VSPTFQVVNS IAPVQECSTQ LDIVIVLDGS
NSIYPWDSVT AFLNDLLERM DIGPKQTQVG IVQYGENVTH EFNLNKYSST EEVLVAAKKI
VQRGGRQTMT ALGIDTARKE AFTEARGARR GVKKVMVIVT DGESHDNHRL KKVIQDCEDE
NIQRFSIAIL GSYNRGNLST EKFVEEIKSI ASEPTEKHFF NVSDELALVT IVKTLGERIF
ALEATADQSA ASFEMEMSQT GFSAHYSQDW VMLGAVGAYD WNGTVVMQKA SQIIIPRNTT
FNVESTKKNE PLASYLGYTV NSATASSGDV LYIAGQPRYN HTGQVIIYRM EDGNIKILQT
LSGEQIGSYF GSILTTTDID KDSNTDILLV GAPMYMGTEK EEQGKVYVYA LNQTRFEYQM
SLEPIKQTCC SSRQHNSCTT ENKNEPCGAR FGTAIAAVKD LNLDGFNDIV IGAPLEDDHG
GAVYIYHGSG KTIRKEYAQR IPSGGDGKTL KFFGQSIHGE MDLNGDGLTD VTIGGLGGAA
LFWSRDVAVV KVTMNFEPNK VNIQKKNCHM EGKETVCINA TVCFDVKLKS KEDTIYEADL
QYRVTLDSLR QISRSFFSGT QERKVQRNIT VRKSECTKHS FYMLDKHDFQ DSVRITLDFN
LTDPENGPVL DDSLPNSVHE YIPFAKDCGN KEKCISDLSL HVATTEKDLL IVRSQNDKFN
VSLTVKNTKD SAYNTRTIVH YSPNLVFSGI EAIQKDSCES NHNITCKVGY PFLRRGEMVT
FKILFQFNTS YLMENVTIYL SATSDSEEPP ETLSDNVVNI SIPVKYEVGL QFYSSASEYH
ISIAANETVP EVINSTEDIG NEINIFYLIR KSGSFPMPEL KLSISFPNMT SNGYPVLYPT
GLSSSENANC RPHIFEDPFS INSGKKMTTS TDHLKRGTIL DCNTCKFATI TCNLTSSDIS
QVNVSLILWK PTFIKSYFSS LNLTIRGELR SENASLVLSS SNQKRELAIQ ISKDGLPGRV
PLWVILLSAF AGLLLLMLLI LALWKIGFFK RPLKKKMEK
