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Disintegrin and metalloproteinase domain-containing protein 17 (ADAM 17) (EC 3.4.24.86) (TNF-alpha convertase) (TNF-alpha-converting enzyme) (CD antigen CD156b)

 ADA17_MOUSE             Reviewed;         827 AA.
Q9Z0F8; O88726; Q505A7; Q9R1U4; Q9Z0K3;
20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 3.
22-NOV-2017, entry version 173.
RecName: Full=Disintegrin and metalloproteinase domain-containing protein 17;
Short=ADAM 17;
EC=3.4.24.86;
AltName: Full=TNF-alpha convertase;
AltName: Full=TNF-alpha-converting enzyme;
AltName: CD_antigen=CD156b;
Flags: Precursor;
Name=Adam17; Synonyms=Tace;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS LONG AND SHORT).
PubMed=10433800; DOI=10.1006/cyto.1998.0466;
Cerretti D.P., Poindexter K., Castner B.J., Means G., Copeland N.G.,
Gilbert D.J., Jenkins N.A., Black R.A., Nelson N.;
"Characterization of the cDNA and gene for mouse tumour necrosis
factor alpha converting enzyme (TACE/ADAM17) and its location to mouse
chromosome 12 and human chromosome 2p25.";
Cytokine 11:541-551(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
PubMed=9755855; DOI=10.1016/S0014-5793(98)01031-X;
Amour A., Slocombe P.M., Webster A., Butler M., Knight C.G.,
Smith B.J., Stephens P.E., Shelley C., Hutton M., Knauper V.,
Docherty A.J., Murphy G.;
"TNF-alpha converting enzyme (TACE) is inhibited by TIMP-3.";
FEBS Lett. 435:39-44(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
PubMed=10375622; DOI=10.1016/S0378-1119(99)00155-9;
Mizui Y., Yamazaki K., Sagane K., Tanaka I.;
"cDNA cloning of mouse tumor necrosis factor-alpha converting enzyme
(TACE) and partial analysis of its promoter.";
Gene 233:67-74(1999).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
Cerretti D.P.;
"Isolation of murine TNF-alpha converting enzyme.";
Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
STRAIN=C57BL/6J; TISSUE=Brain cortex;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
STRAIN=C57BL/6J; TISSUE=Brain;
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]
FUNCTION IN PROCESSING OF GROWTH HORMONE RECEPTOR.
PubMed=11108241; DOI=10.1210/endo.141.12.7858;
Zhang Y., Jiang J., Black R.A., Baumann G., Frank S.J.;
"Tumor necrosis factor-alpha converting enzyme (TACE) is a growth
hormone binding protein (GHBP) sheddase: the metalloprotease
TACE/ADAM-17 is critical for (PMA-induced) GH receptor proteolysis and
GHBP generation.";
Endocrinology 141:4342-4348(2000).
[8]
FUNCTION.
PubMed=10799547; DOI=10.1074/jbc.275.19.14608;
Reddy P., Slack J.L., Davis R., Cerretti D.P., Kozlosky C.J.,
Blanton R.A., Shows D., Peschon J.J., Black R.A.;
"Functional analysis of the domain structure of tumor necrosis factor-
alpha converting enzyme.";
J. Biol. Chem. 275:14608-14614(2000).
[9]
FUNCTION.
PubMed=10882063; DOI=10.1016/S1097-2765(00)80417-7;
Brou C., Logeat F., Gupta N., Bessia C., LeBail O., Doedens J.R.,
Cumano A., Roux P., Black R.A., Israel A.;
"A novel proteolytic cleavage involved in Notch signaling: the role of
the disintegrin-metalloprotease TACE.";
Mol. Cell 5:207-216(2000).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-794, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-735, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, Kidney, Lung, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Cleaves the membrane-bound precursor of TNF-alpha to its
mature soluble form. Responsible for the proteolytical release of
soluble JAM3 from endothelial cells surface. Plays a role in the
proteolytic processing of ACE2 (By similarity). Responsible for
the proteolytic release of several other cell-surface proteins,
including p75 TNF-receptor, interleukin 1 receptor type II, p55
TNF-receptor, transforming growth factor-alpha, L-selectin, growth
hormone receptor, MUC1 and the amyloid precursor protein. Acts as
an activator of Notch pathway by mediating cleavage of Notch,
generating the membrane-associated intermediate fragment called
notch extracellular truncation (NEXT). {ECO:0000250,
ECO:0000269|PubMed:10799547, ECO:0000269|PubMed:10882063,
ECO:0000269|PubMed:11108241}.
-!- CATALYTIC ACTIVITY: Narrow endopeptidase specificity. Cleaves Pro-
Leu-Ala-Gln-Ala-|-Val-Arg-Ser-Ser-Ser in the membrane-bound, 26-
kDa form of tumor necrosis factor alpha (TNF-alpha). Similarly
cleaves other membrane-anchored, cell-surface proteins to 'shed'
the extracellular domains.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000250|UniProtKB:P78536};
Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P78536};
-!- ENZYME REGULATION: Inhibited by metalloproteinase inhibitor 3
(TIMP-3), but not by TIMP-1, TIMP-2 and TIMP-4.
-!- SUBUNIT: Interacts with MAD2L1, MAPK14 and MUC1. {ECO:0000250}.
-!- INTERACTION:
Q80WQ6:Rhbdf2; NbExp=6; IntAct=EBI-7848498, EBI-647271;
-!- SUBCELLULAR LOCATION: Isoform Long: Cell membrane; Single-pass
type I membrane protein.
-!- SUBCELLULAR LOCATION: Isoform Short: Secreted.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Long;
IsoId=Q9Z0F8-1; Sequence=Displayed;
Name=Short;
IsoId=Q9Z0F8-2; Sequence=VSP_005479, VSP_005480;
-!- TISSUE SPECIFICITY: Ubiquitously expressed. Expressed at highest
levels in heart, liver, skeletal muscle, kidney and testes.
Expressed at lower levels in brain, spleen and lung.
-!- DOMAIN: Must be membrane anchored to cleave the different
substrates. The cytoplasmic domain is not required for the this
activity. Only the catalytic domain is essential to shed TNF and
p75 TNFR.
-!- DOMAIN: The conserved cysteine present in the cysteine-switch
motif binds the catalytic zinc ion, thus inhibiting the enzyme.
The dissociation of the cysteine from the zinc ion upon the
activation-peptide release activates the enzyme.
-!- PTM: The precursor is cleaved by a furin endopeptidase.
{ECO:0000250}.
-!- PTM: Phosphorylated. Stimulation by growth factor or phorbol 12-
myristate 13-acetate induces phosphorylation of Ser-822 but
decreases phosphorylation of Ser-794. Phosphorylation at THR-735
by MAPK14 is required for ADAM17-mediated ectodomain shedding (By
similarity). {ECO:0000250}.
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EMBL; AF056359; AAC62934.1; -; Genomic_DNA.
EMBL; AF056345; AAC62934.1; JOINED; Genomic_DNA.
EMBL; AF056346; AAC62934.1; JOINED; Genomic_DNA.
EMBL; AF056347; AAC62934.1; JOINED; Genomic_DNA.
EMBL; AF056348; AAC62934.1; JOINED; Genomic_DNA.
EMBL; AF056349; AAC62934.1; JOINED; Genomic_DNA.
EMBL; AF056350; AAC62934.1; JOINED; Genomic_DNA.
EMBL; AF056351; AAC62934.1; JOINED; Genomic_DNA.
EMBL; AF056352; AAC62934.1; JOINED; Genomic_DNA.
EMBL; AF056353; AAC62934.1; JOINED; Genomic_DNA.
EMBL; AF056354; AAC62934.1; JOINED; Genomic_DNA.
EMBL; AF056355; AAC62934.1; JOINED; Genomic_DNA.
EMBL; AF056356; AAC62934.1; JOINED; Genomic_DNA.
EMBL; AF056357; AAC62934.1; JOINED; Genomic_DNA.
EMBL; AF056358; AAC62934.1; JOINED; Genomic_DNA.
EMBL; AJ007365; CAA07480.1; -; mRNA.
EMBL; AB021709; BAA78578.1; -; mRNA.
EMBL; U69613; AAD09627.1; -; mRNA.
EMBL; U69614; AAD09628.1; -; mRNA.
EMBL; AK139471; BAE24023.1; -; mRNA.
EMBL; BC094655; AAH94655.1; -; mRNA.
CCDS; CCDS25836.1; -. [Q9Z0F8-1]
RefSeq; NP_001264195.1; NM_001277266.1.
RefSeq; NP_001278800.1; NM_001291871.1.
RefSeq; NP_033745.4; NM_009615.6. [Q9Z0F8-1]
UniGene; Mm.27681; -.
ProteinModelPortal; Q9Z0F8; -.
SMR; Q9Z0F8; -.
DIP; DIP-41747N; -.
IntAct; Q9Z0F8; 3.
MINT; MINT-246289; -.
STRING; 10090.ENSMUSP00000067953; -.
BindingDB; Q9Z0F8; -.
ChEMBL; CHEMBL4379; -.
MEROPS; M12.217; -.
iPTMnet; Q9Z0F8; -.
PhosphoSitePlus; Q9Z0F8; -.
SwissPalm; Q9Z0F8; -.
EPD; Q9Z0F8; -.
PaxDb; Q9Z0F8; -.
PeptideAtlas; Q9Z0F8; -.
PRIDE; Q9Z0F8; -.
Ensembl; ENSMUST00000064536; ENSMUSP00000067953; ENSMUSG00000052593. [Q9Z0F8-1]
Ensembl; ENSMUST00000145118; ENSMUSP00000136407; ENSMUSG00000052593. [Q9Z0F8-2]
GeneID; 11491; -.
KEGG; mmu:11491; -.
UCSC; uc007ndu.2; mouse. [Q9Z0F8-1]
CTD; 6868; -.
MGI; MGI:1096335; Adam17.
eggNOG; KOG3658; Eukaryota.
eggNOG; ENOG410XQWB; LUCA.
GeneTree; ENSGT00670000097974; -.
HOGENOM; HOG000033797; -.
HOVERGEN; HBG050457; -.
InParanoid; Q9Z0F8; -.
KO; K06059; -.
TreeFam; TF314733; -.
Reactome; R-MMU-193692; Regulated proteolysis of p75NTR.
Reactome; R-MMU-75893; TNF signaling.
PMAP-CutDB; Q505A7; -.
PRO; PR:Q9Z0F8; -.
Proteomes; UP000000589; Chromosome 12.
Bgee; ENSMUSG00000052593; -.
CleanEx; MM_ADAM17; -.
ExpressionAtlas; Q9Z0F8; baseline and differential.
Genevisible; Q9Z0F8; MM.
GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
GO; GO:0009986; C:cell surface; ISO:MGI.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:0045121; C:membrane raft; ISO:MGI.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0005178; F:integrin binding; ISO:MGI.
GO; GO:0005138; F:interleukin-6 receptor binding; ISO:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004222; F:metalloendopeptidase activity; ISO:MGI.
GO; GO:0008237; F:metallopeptidase activity; IDA:BHF-UCL.
GO; GO:0005112; F:Notch binding; ISS:UniProtKB.
GO; GO:0030165; F:PDZ domain binding; ISO:MGI.
GO; GO:0004252; F:serine-type endopeptidase activity; TAS:Reactome.
GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
GO; GO:0030183; P:B cell differentiation; IMP:BHF-UCL.
GO; GO:0007155; P:cell adhesion; ISO:MGI.
GO; GO:0033627; P:cell adhesion mediated by integrin; ISO:MGI.
GO; GO:0048870; P:cell motility; IMP:BHF-UCL.
GO; GO:0050830; P:defense response to Gram-positive bacterium; ISO:MGI.
GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; ISO:MGI.
GO; GO:0035625; P:epidermal growth factor-activated receptor transactivation by G-protein coupled receptor signaling pathway; ISO:MGI.
GO; GO:0002467; P:germinal center formation; IMP:BHF-UCL.
GO; GO:0060397; P:JAK-STAT cascade involved in growth hormone signaling pathway; TAS:Reactome.
GO; GO:0006509; P:membrane protein ectodomain proteolysis; IDA:MGI.
GO; GO:0010977; P:negative regulation of neuron projection development; IGI:MGI.
GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; ISO:MGI.
GO; GO:0007220; P:Notch receptor processing; ISS:UniProtKB.
GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
GO; GO:0051088; P:PMA-inducible membrane protein ectodomain proteolysis; IDA:BHF-UCL.
GO; GO:0030307; P:positive regulation of cell growth; ISO:MGI.
GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
GO; GO:0008284; P:positive regulation of cell proliferation; ISO:MGI.
GO; GO:0051272; P:positive regulation of cellular component movement; IMP:BHF-UCL.
GO; GO:0032722; P:positive regulation of chemokine production; ISO:MGI.
GO; GO:0031659; P:positive regulation of cyclin-dependent protein serine/threonine kinase activity involved in G1/S transition of mitotic cell cycle; ISO:MGI.
GO; GO:0045741; P:positive regulation of epidermal growth factor-activated receptor activity; ISO:MGI.
GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
GO; GO:0010820; P:positive regulation of T cell chemotaxis; ISO:MGI.
GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; IMP:BHF-UCL.
GO; GO:0002532; P:production of molecular mediator involved in inflammatory response; IDA:CACAO.
GO; GO:0006508; P:proteolysis; ISS:UniProtKB.
GO; GO:0048679; P:regulation of axon regeneration; IGI:MGI.
GO; GO:0033025; P:regulation of mast cell apoptotic process; IMP:BHF-UCL.
GO; GO:2001222; P:regulation of neuron migration; IGI:MGI.
GO; GO:0042493; P:response to drug; IMP:BHF-UCL.
GO; GO:0055099; P:response to high density lipoprotein particle; ISO:MGI.
GO; GO:0001666; P:response to hypoxia; ISO:MGI.
GO; GO:0032496; P:response to lipopolysaccharide; ISO:MGI.
GO; GO:0048536; P:spleen development; IMP:BHF-UCL.
GO; GO:0033077; P:T cell differentiation in thymus; IMP:BHF-UCL.
CDD; cd14246; ADAM17_MPD; 1.
CDD; cd04270; ZnMc_TACE_like; 1.
Gene3D; 3.40.390.10; -; 1.
Gene3D; 4.10.70.10; -; 1.
InterPro; IPR034025; ADAM10_ADAM17.
InterPro; IPR032029; ADAM17_MPD.
InterPro; IPR001762; Disintegrin_dom.
InterPro; IPR036436; Disintegrin_dom_sf.
InterPro; IPR024079; MetalloPept_cat_dom_sf.
InterPro; IPR001590; Peptidase_M12B.
InterPro; IPR002870; Peptidase_M12B_N.
Pfam; PF16698; ADAM17_MPD; 1.
Pfam; PF00200; Disintegrin; 1.
Pfam; PF01562; Pep_M12B_propep; 1.
SMART; SM00050; DISIN; 1.
SUPFAM; SSF57552; SSF57552; 1.
PROSITE; PS50215; ADAM_MEPRO; 1.
PROSITE; PS50214; DISINTEGRIN_2; 1.
PROSITE; PS00142; ZINC_PROTEASE; 1.
1: Evidence at protein level;
Alternative splicing; Cell membrane;
Cleavage on pair of basic residues; Complete proteome; Disulfide bond;
Glycoprotein; Hydrolase; Membrane; Metal-binding; Metalloprotease;
Notch signaling pathway; Phosphoprotein; Protease; Reference proteome;
Secreted; SH3-binding; Signal; Transmembrane; Transmembrane helix;
Zinc; Zymogen.
SIGNAL 1 17 {ECO:0000250|UniProtKB:Q9Z1K9}.
PROPEP 18 214 {ECO:0000250|UniProtKB:P78536}.
/FTId=PRO_0000029090.
CHAIN 215 827 Disintegrin and metalloproteinase domain-
containing protein 17.
/FTId=PRO_0000029091.
TOPO_DOM 215 671 Extracellular. {ECO:0000255}.
TRANSMEM 672 692 Helical. {ECO:0000255}.
TOPO_DOM 693 827 Cytoplasmic. {ECO:0000255}.
DOMAIN 223 474 Peptidase M12B. {ECO:0000255|PROSITE-
ProRule:PRU00276}.
DOMAIN 475 563 Disintegrin. {ECO:0000255|PROSITE-
ProRule:PRU00068}.
REGION 603 671 Crambin-like.
MOTIF 182 189 Cysteine switch. {ECO:0000250}.
MOTIF 731 738 SH3-binding. {ECO:0000255}.
COMPBIAS 96 99 Poly-Val.
COMPBIAS 564 602 Cys-rich.
ACT_SITE 406 406 {ECO:0000255|PROSITE-ProRule:PRU00276,
ECO:0000255|PROSITE-ProRule:PRU10095}.
METAL 184 184 Zinc; in inhibited form. {ECO:0000250}.
METAL 405 405 Zinc; catalytic.
{ECO:0000250|UniProtKB:P78536}.
METAL 409 409 Zinc; catalytic.
{ECO:0000250|UniProtKB:P78536}.
METAL 415 415 Zinc; catalytic.
{ECO:0000250|UniProtKB:P78536}.
MOD_RES 735 735 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 764 764 Phosphothreonine.
{ECO:0000250|UniProtKB:P78536}.
MOD_RES 770 770 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Z1K9}.
MOD_RES 794 794 Phosphoserine.
{ECO:0000244|PubMed:19144319}.
MOD_RES 822 822 Phosphoserine.
{ECO:0000250|UniProtKB:P78536}.
CARBOHYD 157 157 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 264 264 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 452 452 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 498 498 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 539 539 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 551 551 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 606 606 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 225 333 {ECO:0000250|UniProtKB:P78536}.
DISULFID 365 469 {ECO:0000250|UniProtKB:P78536}.
DISULFID 423 453 {ECO:0000250|UniProtKB:P78536}.
DISULFID 534 555 {ECO:0000250}.
DISULFID 573 582 {ECO:0000250}.
DISULFID 578 591 {ECO:0000250}.
DISULFID 593 600 {ECO:0000250}.
VAR_SEQ 639 655 GKCEKRVQDVIERFWDF -> CDFFSPYRANVRNEYRT
(in isoform Short). {ECO:0000303|Ref.4}.
/FTId=VSP_005479.
VAR_SEQ 656 827 Missing (in isoform Short).
{ECO:0000303|Ref.4}.
/FTId=VSP_005480.
CONFLICT 3 4 RR -> QS (in Ref. 2; CAA07480).
{ECO:0000305}.
CONFLICT 7 7 I -> F (in Ref. 2; CAA07480).
{ECO:0000305}.
CONFLICT 28 28 S -> A (in Ref. 2; CAA07480 and 3;
BAA78578). {ECO:0000305}.
CONFLICT 113 113 N -> D (in Ref. 1; AAC62934, 2; CAA07480,
3; BAA78578 and 4; AAD09627/AAD09628).
{ECO:0000305}.
CONFLICT 149 149 V -> I (in Ref. 2; CAA07480 and 3;
BAA78578). {ECO:0000305}.
CONFLICT 594 594 V -> I (in Ref. 1; AAC62934 and 4;
AAD09627/AAD09628). {ECO:0000305}.
CONFLICT 752 752 P -> S (in Ref. 2; CAA07480 and 3;
BAA78578). {ECO:0000305}.
CONFLICT 775 775 A -> V (in Ref. 2; CAA07480 and 3;
BAA78578). {ECO:0000305}.
SEQUENCE 827 AA; 93056 MW; 6B434F80878197F5 CRC64;
MRRRLLILTT LVPFVLAPRP PEEAGSGSHP RLEKLDSLLS DYDILSLANI QQHSIRKRDL
QSATHLETLL TFSALKRHFK LYLTSSTERF SQNLRVVVVD GKEESEYSVK WQNFFSGHVV
GEPDSRVLAH IGDDDVTVRI NTDGAEYNVE PLWRFVNDTK DKRMLVYKSE DIKDFSRLQS
PKVCGYLNAD SEELLPKGLI DREPSEEFVR RVKRRAEPNP LKNTCKLLVV ADHRFYKYMG
RGEESTTTNY LIELIDRVDD IYRNTSWDNA GFKGYGVQIE QIRILKSPQE VKPGERHFNM
AKSFPNEEKD AWDVKMLLEQ FSFDIAEEAS KVCLAHLFTY QDFDMGTLGL AYVGSPRANS
HGGVCPKAYY NPTVKKNIYL NSGLTSTKNY GKTILTKEAD LVTTHELGHN FGAEHDPDGL
AECAPNEDQG GKYVMYPIAV SGDHENNKMF SNCSKQSIYK TIESKAQECF QERSNKVCGN
SRVDEGEECD PGIMYLNNDT CCNSDCTLKP GVQCSDRNSP CCKNCQFETA QKKCQEAINA
TCKGVSYCTG NSSECPPPGD AEDDTVCLDL GKCKAGKCIP FCKREQELES CACVDTDNSC
KVCCRNLSGP CVPYVDAEQK NLFLRKGKPC TVGFCDMNGK CEKRVQDVIE RFWDFIDQLS
INTFGKFLAD NIVGSVLVFS LIFWIPFSIL VHCVDKKLDK QYESLSLFHH SNIEMLSSMD
SASVRIIKPF PAPQTPGRLQ ALQPAAMMPP VPAAPKLDHQ RMDTIQEDPS TDSHADDDGF
EKDPFPNSST AAKSFEDLTD HPVTRSEKAA SFKLQRQSRV DSKETEC


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