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Integrin beta-6

 ITB6_HUMAN              Reviewed;         788 AA.
P18564; B2R9W5; C9JA97; Q0VA95; Q16500; Q53RG5; Q53RR6;
01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
27-APR-2001, sequence version 2.
25-OCT-2017, entry version 184.
RecName: Full=Integrin beta-6;
Flags: Precursor;
Name=ITGB6;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Pancreas;
PubMed=2365683;
Sheppard D., Rozzo C., Starr L., Quaranta V., Erle D.J., Pytela R.;
"Complete amino acid sequence of a novel integrin beta subunit (beta
6) identified in epithelial cells using the polymerase chain
reaction.";
J. Biol. Chem. 265:11502-11507(1990).
[2]
SEQUENCE REVISION TO 18-24; 158; 642 AND 719.
Askins J.;
Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Placenta;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 116-197.
PubMed=1382574; DOI=10.1093/intimm/4.9.1031;
Jiang W.-M., Jenkins D., Yuan Q., Leung E., Choo K.H., Watson J.D.,
Krissansen G.W.;
"The gene organization of the human beta 7 subunit, the common beta
subunit of the leukocyte integrins HML-1 and LPAM-1.";
Int. Immunol. 4:1031-1040(1992).
[8]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH COXSACKIEVIRUS B1
CAPSID PROTEINS.
PubMed=9426447; DOI=10.1006/viro.1997.8831;
Agrez M.V., Shafren D.R., Gu X., Cox K., Sheppard D., Barry R.D.;
"Integrin alpha v beta 6 enhances coxsackievirus B1 lytic infection of
human colon cancer cells.";
Virology 239:71-77(1997).
[9]
INTERACTION WITH FLNB.
TISSUE=Keratinocyte, and Skeletal muscle;
PubMed=11807098; DOI=10.1083/jcb.200103037;
van Der Flier A., Kuikman I., Kramer D., Geerts D., Kreft M.,
Takafuta T., Shapiro S.S., Sonnenberg A.;
"Different splice variants of filamin-B affect myogenesis, subcellular
distribution, and determine binding to integrin (beta) subunits.";
J. Cell Biol. 156:361-376(2002).
[10]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH COXSACKIEVIRUS A9
CAPSID PROTEINS.
PubMed=15194773; DOI=10.1128/JVI.78.13.6967-6973.2004;
Williams C.H., Kajander T., Hyypia T., Jackson T., Sheppard D.,
Stanway G.;
"Integrin alpha v beta 6 is an RGD-dependent receptor for
coxsackievirus A9.";
J. Virol. 78:6967-6973(2004).
[11]
INTERACTION WITH HAX1, AND FUNCTION.
PubMed=17545607; DOI=10.1158/0008-5472.CAN-07-0318;
Ramsay A.G., Keppler M.D., Jazayeri M., Thomas G.J., Parsons M.,
Violette S., Weinreb P., Hart I.R., Marshall J.F.;
"HS1-associated protein X-1 regulates carcinoma cell migration and
invasion via clathrin-mediated endocytosis of integrin alphavbeta6.";
Cancer Res. 67:5275-5284(2007).
[12]
FUNCTION, INTERACTION WITH FBN1, AND SUBCELLULAR LOCATION.
PubMed=17158881; DOI=10.1074/jbc.M607008200;
Jovanovic J., Takagi J., Choulier L., Abrescia N.G., Stuart D.I.,
van der Merwe P.A., Mardon H.J., Handford P.A.;
"alphaVbeta6 is a novel receptor for human fibrillin-1. Comparative
studies of molecular determinants underlying integrin-rgd affinity and
specificity.";
J. Biol. Chem. 282:6743-6751(2007).
[13]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HERPES
SIMPLES-1/HHV-1 GH:GL PROTEINS.
PubMed=24367260; DOI=10.1371/journal.ppat.1003806;
Gianni T., Salvioli S., Chesnokova L.S., Hutt-Fletcher L.M.,
Campadelli-Fiume G.;
"alphavbeta6- and alphavbeta8-integrins serve as interchangeable
receptors for HSV gH/gL to promote endocytosis and activation of
membrane fusion.";
PLoS Pathog. 9:E1003806-E1003806(2013).
[14]
INVOLVEMENT IN AI1H, AND VARIANT AI1H THR-196.
PubMed=24319098; DOI=10.1093/hmg/ddt616;
Poulter J.A., Brookes S.J., Shore R.C., Smith C.E., Abi Farraj L.,
Kirkham J., Inglehearn C.F., Mighell A.J.;
"A missense mutation in ITGB6 causes pitted hypomineralized
amelogenesis imperfecta.";
Hum. Mol. Genet. 23:2189-2197(2014).
[15]
INVOLVEMENT IN AI1H, AND VARIANTS AI1H THR-143 AND GLN-275.
PubMed=24305999; DOI=10.1093/hmg/ddt611;
Wang S.K., Choi M., Richardson A.S., Reid B.M., Lin B.P., Wang S.J.,
Kim J.W., Simmer J.P., Hu J.C.;
"ITGB6 loss-of-function mutations cause autosomal recessive
amelogenesis imperfecta.";
Hum. Mol. Genet. 23:2157-2163(2014).
-!- FUNCTION: Integrin alpha-V/beta-6 is a receptor for fibronectin
and cytotactin. It recognizes the sequence R-G-D in its ligands.
Internalisation of integrin alpha-V/beta-6 via clathrin-mediated
endocytosis promotes carcinoma cell invasion. ITGAV:ITGB6 acts as
a receptor for fibrillin-1 (FBN1) and mediates R-G-D-dependent
cell adhesion to FBN1 (PubMed:17158881).
{ECO:0000269|PubMed:17158881, ECO:0000269|PubMed:17545607}.
-!- FUNCTION: (Microbial infection) Integrin ITGAV:ITGB6 acts as a
receptor for coxsackievirus A9 and coxsackievirus B1
(PubMed:9426447, PubMed:15194773). Integrin ITGAV:ITGB6 acts as a
receptor for herpes simplex virus-1/HHV-1 (PubMed:24367260).
{ECO:0000269|PubMed:15194773, ECO:0000269|PubMed:24367260,
ECO:0000269|PubMed:9426447}.
-!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Beta-6
associates with alpha-V. Interacts with FLNB. Interacts with HAX1.
ITGAV:ITGB6 interacts with FBN1 (PubMed:17158881).
{ECO:0000269|PubMed:11807098, ECO:0000269|PubMed:17158881,
ECO:0000269|PubMed:17545607}.
-!- SUBUNIT: (Microbial infection) Integrin ITGAV:ITGB6 interacts with
coxsackievirus A9, coxsackievirus B1 capsid proteins
(PubMed:9426447, PubMed:15194773). {ECO:0000269|PubMed:15194773,
ECO:0000269|PubMed:9426447}.
-!- SUBUNIT: (Microbial infection) Integrin ITGAV:ITGB6 interacts with
herpes simplex virus-1/HHV-1 gH:gL proteins.
{ECO:0000269|PubMed:24367260}.
-!- INTERACTION:
P06756:ITGAV; NbExp=7; IntAct=EBI-2568070, EBI-298282;
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein. Cell junction, focal adhesion
{ECO:0000269|PubMed:17158881}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P18564-1; Sequence=Displayed;
Name=2;
IsoId=P18564-2; Sequence=VSP_055189;
Note=No experimental confirmation available. Gene prediction
confirmed by EST data.;
-!- DISEASE: Amelogenesis imperfecta 1H (AI1H) [MIM:616221]: A
disorder characterized by defective enamel formation, resulting in
hypoplastic and hypomineralized tooth enamel that may be rough,
pitted, and/or discolored. {ECO:0000269|PubMed:24305999,
ECO:0000269|PubMed:24319098}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the integrin beta chain family.
{ECO:0000305}.
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EMBL; M35198; AAA36122.2; -; mRNA.
EMBL; AC092153; AAX93093.1; -; Genomic_DNA.
EMBL; AK313944; BAG36662.1; -; mRNA.
EMBL; AC080166; AAY24053.1; -; Genomic_DNA.
EMBL; CH471058; EAX11390.1; -; Genomic_DNA.
EMBL; BC121178; AAI21179.1; -; mRNA.
EMBL; S49380; AAB23690.1; -; Genomic_DNA.
CCDS; CCDS2212.1; -. [P18564-1]
CCDS; CCDS63040.1; -. [P18564-2]
PIR; A37057; A37057.
RefSeq; NP_000879.2; NM_000888.4. [P18564-1]
RefSeq; NP_001269282.1; NM_001282353.1. [P18564-1]
RefSeq; NP_001269284.1; NM_001282355.1. [P18564-2]
RefSeq; NP_001269317.1; NM_001282388.1.
UniGene; Hs.470399; -.
PDB; 1LH9; Model; -; A=76-546.
PDB; 4UM8; X-ray; 2.85 A; B/D=1-788.
PDB; 4UM9; X-ray; 2.50 A; B/D=18-491.
PDB; 5FFG; X-ray; 2.25 A; B=128-378.
PDB; 5FFO; X-ray; 3.49 A; B/F=128-378.
PDB; 5NEM; EM; 3.10 A; B=22-491.
PDB; 5NER; EM; 3.10 A; B=22-491.
PDB; 5NET; EM; 3.10 A; B=22-491.
PDB; 5NEU; EM; 3.10 A; B=22-491.
PDBsum; 1LH9; -.
PDBsum; 4UM8; -.
PDBsum; 4UM9; -.
PDBsum; 5FFG; -.
PDBsum; 5FFO; -.
PDBsum; 5NEM; -.
PDBsum; 5NER; -.
PDBsum; 5NET; -.
PDBsum; 5NEU; -.
ProteinModelPortal; P18564; -.
SMR; P18564; -.
BioGrid; 109900; 5.
CORUM; P18564; -.
DIP; DIP-59187N; -.
ELM; P18564; -.
IntAct; P18564; 1.
STRING; 9606.ENSP00000283249; -.
BindingDB; P18564; -.
ChEMBL; CHEMBL2111416; -.
iPTMnet; P18564; -.
PhosphoSitePlus; P18564; -.
DMDM; 13432176; -.
EPD; P18564; -.
MaxQB; P18564; -.
PaxDb; P18564; -.
PeptideAtlas; P18564; -.
PRIDE; P18564; -.
DNASU; 3694; -.
Ensembl; ENST00000283249; ENSP00000283249; ENSG00000115221. [P18564-1]
Ensembl; ENST00000409872; ENSP00000386367; ENSG00000115221. [P18564-1]
Ensembl; ENST00000409967; ENSP00000386828; ENSG00000115221. [P18564-2]
GeneID; 3694; -.
KEGG; hsa:3694; -.
UCSC; uc010fou.4; human. [P18564-1]
CTD; 3694; -.
DisGeNET; 3694; -.
EuPathDB; HostDB:ENSG00000115221.10; -.
GeneCards; ITGB6; -.
GeneCards; LINC02478; -.
HGNC; HGNC:6161; ITGB6.
HPA; CAB073536; -.
HPA; HPA023626; -.
MalaCards; ITGB6; -.
MIM; 147558; gene.
MIM; 616221; phenotype.
neXtProt; NX_P18564; -.
OpenTargets; ENSG00000115221; -.
Orphanet; 100032; Hypocalcified amelogenesis imperfecta.
Orphanet; 100031; Hypoplastic amelogenesis imperfecta.
PharmGKB; PA29960; -.
eggNOG; KOG1226; Eukaryota.
eggNOG; ENOG410XP60; LUCA.
GeneTree; ENSGT00760000119064; -.
HOGENOM; HOG000252936; -.
HOVERGEN; HBG006190; -.
InParanoid; P18564; -.
KO; K06589; -.
OMA; GEYCNCT; -.
OrthoDB; EOG091G029W; -.
PhylomeDB; P18564; -.
TreeFam; TF105392; -.
Reactome; R-HSA-1566948; Elastic fibre formation.
Reactome; R-HSA-2129379; Molecules associated with elastic fibres.
Reactome; R-HSA-216083; Integrin cell surface interactions.
Reactome; R-HSA-3000178; ECM proteoglycans.
SignaLink; P18564; -.
SIGNOR; P18564; -.
GeneWiki; Integrin,_beta_6; -.
GenomeRNAi; 3694; -.
PRO; PR:P18564; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000115221; -.
CleanEx; HS_ITGB6; -.
ExpressionAtlas; P18564; baseline and differential.
Genevisible; P18564; HS.
GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0034685; C:integrin alphav-beta6 complex; IEA:Ensembl.
GO; GO:0008305; C:integrin complex; TAS:ProtInc.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0043235; C:receptor complex; IDA:MGI.
GO; GO:0005178; F:integrin binding; IEA:Ensembl.
GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
GO; GO:0033627; P:cell adhesion mediated by integrin; IDA:UniProtKB.
GO; GO:0007160; P:cell-matrix adhesion; IEA:InterPro.
GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
GO; GO:0038044; P:transforming growth factor-beta secretion; IEA:Ensembl.
Gene3D; 1.20.5.100; -; 1.
Gene3D; 1.20.5.630; -; 1.
InterPro; IPR021157; Cyt_c1_TM_anchor_C.
InterPro; IPR013111; EGF_extracell.
InterPro; IPR033760; Integrin_beta_N.
InterPro; IPR015812; Integrin_bsu.
InterPro; IPR015436; Integrin_bsu-6.
InterPro; IPR014836; Integrin_bsu_cyt_dom.
InterPro; IPR037076; Integrin_bsu_cyt_dom_sf.
InterPro; IPR012896; Integrin_bsu_tail.
InterPro; IPR036349; Integrin_bsu_tail_dom_sf.
InterPro; IPR002369; Integrin_bsu_VWA.
InterPro; IPR032695; Integrin_dom.
InterPro; IPR016201; PSI.
InterPro; IPR036465; vWFA_dom_sf.
PANTHER; PTHR10082; PTHR10082; 1.
PANTHER; PTHR10082:SF11; PTHR10082:SF11; 1.
Pfam; PF07974; EGF_2; 2.
Pfam; PF08725; Integrin_b_cyt; 1.
Pfam; PF07965; Integrin_B_tail; 1.
Pfam; PF00362; Integrin_beta; 1.
Pfam; PF17205; PSI_integrin; 1.
PIRSF; PIRSF002512; Integrin_B; 1.
PRINTS; PR01186; INTEGRINB.
SMART; SM00187; INB; 1.
SMART; SM01241; Integrin_b_cyt; 1.
SMART; SM01242; Integrin_B_tail; 1.
SMART; SM00423; PSI; 1.
SUPFAM; SSF53300; SSF53300; 1.
SUPFAM; SSF69179; SSF69179; 2.
SUPFAM; SSF69687; SSF69687; 1.
PROSITE; PS00022; EGF_1; 2.
PROSITE; PS01186; EGF_2; 1.
PROSITE; PS00243; INTEGRIN_BETA; 3.
1: Evidence at protein level;
3D-structure; Alternative splicing; Amelogenesis imperfecta;
Cell adhesion; Cell junction; Complete proteome; Disease mutation;
Disulfide bond; Glycoprotein; Host cell receptor for virus entry;
Host-virus interaction; Integrin; Membrane; Polymorphism; Receptor;
Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 21 {ECO:0000255}.
CHAIN 22 788 Integrin beta-6.
/FTId=PRO_0000016350.
TOPO_DOM 22 709 Extracellular. {ECO:0000255}.
TRANSMEM 710 730 Helical. {ECO:0000255}.
TOPO_DOM 731 788 Cytoplasmic. {ECO:0000255}.
DOMAIN 131 371 VWFA.
REPEAT 456 501 I.
REPEAT 502 543 II.
REPEAT 544 582 III.
REPEAT 583 619 IV.
REGION 456 619 Cysteine-rich tandem repeats.
REGION 731 758 Interaction with HAX1.
{ECO:0000269|PubMed:17545607}.
CARBOHYD 48 48 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 97 97 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 260 260 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 387 387 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 396 396 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 463 463 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 471 471 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 541 541 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 575 575 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 23 454 {ECO:0000250}.
DISULFID 31 41 {ECO:0000250}.
DISULFID 34 70 {ECO:0000250}.
DISULFID 44 59 {ECO:0000250}.
DISULFID 197 204 {ECO:0000250}.
DISULFID 252 293 {ECO:0000250}.
DISULFID 394 406 {ECO:0000250}.
DISULFID 426 670 {ECO:0000250}.
DISULFID 452 456 {ECO:0000250}.
DISULFID 467 479 {ECO:0000250}.
DISULFID 476 511 {ECO:0000250}.
DISULFID 481 490 {ECO:0000250}.
DISULFID 492 502 {ECO:0000250}.
DISULFID 517 522 {ECO:0000250}.
DISULFID 519 552 {ECO:0000250}.
DISULFID 524 537 {ECO:0000250}.
DISULFID 539 544 {ECO:0000250}.
DISULFID 558 563 {ECO:0000250}.
DISULFID 560 591 {ECO:0000250}.
DISULFID 565 574 {ECO:0000250}.
DISULFID 576 583 {ECO:0000250}.
DISULFID 597 602 {ECO:0000250}.
DISULFID 599 645 {ECO:0000250}.
DISULFID 604 614 {ECO:0000250}.
DISULFID 617 620 {ECO:0000250}.
DISULFID 624 633 {ECO:0000250}.
DISULFID 630 702 {ECO:0000250}.
DISULFID 649 678 {ECO:0000250}.
VAR_SEQ 554 660 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_055189.
VARIANT 143 143 A -> T (in AI1H; dbSNP:rs140015315).
{ECO:0000269|PubMed:24305999}.
/FTId=VAR_073328.
VARIANT 196 196 P -> T (in AI1H; dbSNP:rs730880298).
{ECO:0000269|PubMed:24319098}.
/FTId=VAR_073329.
VARIANT 275 275 H -> Q (in AI1H; dbSNP:rs730882118).
{ECO:0000269|PubMed:24305999}.
/FTId=VAR_073330.
VARIANT 437 437 P -> T (in dbSNP:rs2305820).
/FTId=VAR_049636.
TURN 24 26 {ECO:0000244|PDB:4UM9}.
HELIX 31 34 {ECO:0000244|PDB:4UM9}.
STRAND 42 44 {ECO:0000244|PDB:4UM9}.
HELIX 62 68 {ECO:0000244|PDB:4UM9}.
TURN 72 74 {ECO:0000244|PDB:4UM9}.
STRAND 81 86 {ECO:0000244|PDB:4UM9}.
HELIX 98 100 {ECO:0000244|PDB:4UM9}.
STRAND 108 113 {ECO:0000244|PDB:4UM9}.
STRAND 119 126 {ECO:0000244|PDB:4UM9}.
STRAND 133 140 {ECO:0000244|PDB:5FFG}.
HELIX 143 145 {ECO:0000244|PDB:5FFG}.
HELIX 146 151 {ECO:0000244|PDB:5FFG}.
HELIX 152 154 {ECO:0000244|PDB:5FFG}.
HELIX 155 166 {ECO:0000244|PDB:5FFG}.
STRAND 170 177 {ECO:0000244|PDB:5FFG}.
TURN 183 185 {ECO:0000244|PDB:4UM9}.
HELIX 190 194 {ECO:0000244|PDB:5FFG}.
TURN 196 201 {ECO:0000244|PDB:5FFG}.
STRAND 209 218 {ECO:0000244|PDB:5FFG}.
HELIX 220 229 {ECO:0000244|PDB:5FFG}.
STRAND 236 241 {ECO:0000244|PDB:4UM9}.
HELIX 242 251 {ECO:0000244|PDB:5FFG}.
HELIX 253 256 {ECO:0000244|PDB:5FFG}.
STRAND 262 272 {ECO:0000244|PDB:5FFG}.
HELIX 277 283 {ECO:0000244|PDB:5FFG}.
STRAND 297 301 {ECO:0000244|PDB:5FFG}.
TURN 302 306 {ECO:0000244|PDB:5FFG}.
HELIX 312 321 {ECO:0000244|PDB:5FFG}.
STRAND 324 330 {ECO:0000244|PDB:5FFG}.
HELIX 332 344 {ECO:0000244|PDB:5FFG}.
STRAND 349 352 {ECO:0000244|PDB:5FFG}.
HELIX 360 371 {ECO:0000244|PDB:5FFG}.
STRAND 375 382 {ECO:0000244|PDB:4UM9}.
STRAND 387 393 {ECO:0000244|PDB:4UM9}.
TURN 395 397 {ECO:0000244|PDB:4UM8}.
STRAND 399 401 {ECO:0000244|PDB:4UM9}.
STRAND 414 422 {ECO:0000244|PDB:4UM9}.
STRAND 431 437 {ECO:0000244|PDB:4UM9}.
STRAND 444 450 {ECO:0000244|PDB:4UM9}.
HELIX 455 457 {ECO:0000244|PDB:4UM8}.
STRAND 467 475 {ECO:0000244|PDB:4UM9}.
STRAND 478 481 {ECO:0000244|PDB:4UM9}.
SEQUENCE 788 AA; 85936 MW; EDB7D533EC4C8C4D CRC64;
MGIELLCLFF LFLGRNDHVQ GGCALGGAET CEDCLLIGPQ CAWCAQENFT HPSGVGERCD
TPANLLAKGC QLNFIENPVS QVEILKNKPL SVGRQKNSSD IVQIAPQSLI LKLRPGGAQT
LQVHVRQTED YPVDLYYLMD LSASMDDDLN TIKELGSRLS KEMSKLTSNF RLGFGSFVEK
PVSPFVKTTP EEIANPCSSI PYFCLPTFGF KHILPLTNDA ERFNEIVKNQ KISANIDTPE
GGFDAIMQAA VCKEKIGWRN DSLHLLVFVS DADSHFGMDS KLAGIVIPND GLCHLDSKNE
YSMSTVLEYP TIGQLIDKLV QNNVLLIFAV TQEQVHLYEN YAKLIPGATV GLLQKDSGNI
LQLIISAYEE LRSEVELEVL GDTEGLNLSF TAICNNGTLF QHQKKCSHMK VGDTASFSVT
VNIPHCERRS RHIIIKPVGL GDALELLVSP ECNCDCQKEV EVNSSKCHHG NGSFQCGVCA
CHPGHMGPRC ECGEDMLSTD SCKEAPDHPS CSGRGDCYCG QCICHLSPYG NIYGPYCQCD
NFSCVRHKGL LCGGNGDCDC GECVCRSGWT GEYCNCTTST DSCVSEDGVL CSGRGDCVCG
KCVCTNPGAS GPTCERCPTC GDPCNSKRSC IECHLSAAGQ AREECVDKCK LAGATISEEE
DFSKDGSVSC SLQGENECLI TFLITTDNEG KTIIHSINEK DCPKPPNIPM IMLGVSLAIL
LIGVVLLCIW KLLVSFHDRK EVAKFEAERS KAKWQTGTNP LYRGSTSTFK NVTYKHREKQ
KVDLSTDC


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