ADAM9_HUMAN
ID ADAM9_HUMAN Reviewed; 819 AA.
AC Q13443; B7ZLN7; Q10718; Q8NFM6;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 210.
DE RecName: Full=Disintegrin and metalloproteinase domain-containing protein 9;
DE Short=ADAM 9;
DE EC=3.4.24.-;
DE AltName: Full=Cellular disintegrin-related protein;
DE AltName: Full=Meltrin-gamma;
DE AltName: Full=Metalloprotease/disintegrin/cysteine-rich protein 9;
DE AltName: Full=Myeloma cell metalloproteinase;
DE Flags: Precursor;
GN Name=ADAM9; Synonyms=KIAA0021, MCMP, MDC9, MLTNG;
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 [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Mammary carcinoma;
RX PubMed=8647900; DOI=10.1083/jcb.132.4.717;
RA Weskamp G., Kraetzschmar J., Reid M.S., Blobel C.P.;
RT "MDC9, a widely expressed cellular disintegrin containing cytoplasmic SH3
RT ligand domains.";
RL J. Cell Biol. 132:717-726(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=8809033; DOI=10.1042/bj3180459;
RA McKie N., Dallas D.J., Edwards T., Apperley J.F., Russell R.G.G.,
RA Croucher P.I.;
RT "Cloning of a novel membrane-linked metalloproteinase from human myeloma
RT cells.";
RL Biochem. J. 318:459-462(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=12054541; DOI=10.1016/s0006-291x(02)00302-9;
RA Hotoda N., Koike H., Sasagawa N., Ishiura S.;
RT "A secreted form of human ADAM9 has an alpha-secretase activity for APP.";
RL Biochem. Biophys. Res. Commun. 293:800-805(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Bone marrow;
RX PubMed=7584026; DOI=10.1093/dnares/1.1.27;
RA Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y., Sato S.,
RA Nagase T., Seki N., Ishikawa K., Tabata S.;
RT "Prediction of the coding sequences of unidentified human genes. I. The
RT coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of
RT randomly sampled cDNA clones from human immature myeloid cell line KG-1.";
RL DNA Res. 1:27-35(1994).
RN [5]
RP SEQUENCE REVISION.
RA Ohara O., Nagase T., Kikuno R., Nomura N.;
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Lung;
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 [8]
RP TISSUE SPECIFICITY.
RX PubMed=9016778; DOI=10.1006/bbrc.1996.5957;
RA McKie N., Edwards T., Dallas D.J., Houghton A., Stringer B., Graham R.,
RA Russell G., Croucher P.I.;
RT "Expression of members of a novel membrane linked metalloproteinase family
RT (ADAM) in human articular chondrocytes.";
RL Biochem. Biophys. Res. Commun. 230:335-339(1997).
RN [9]
RP INTERACTION WITH SH3GL2 AND SNX9.
RX PubMed=10531379; DOI=10.1074/jbc.274.44.31693;
RA Howard L., Nelson K.K., Maciewicz R.A., Blobel C.P.;
RT "Interaction of the metalloprotease disintegrins MDC9 and MDC15 with two
RT SH3 domain-containing proteins, endophilin I and SH3PX1.";
RL J. Biol. Chem. 274:31693-31699(1999).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP INVOLVEMENT IN CORD9.
RX PubMed=19409519; DOI=10.1016/j.ajhg.2009.04.005;
RA Parry D.A., Toomes C., Bida L., Danciger M., Towns K.V., McKibbin M.,
RA Jacobson S.G., Logan C.V., Ali M., Bond J., Chance R., Swendeman S.,
RA Daniele L.L., Springell K., Adams M., Johnson C.A., Booth A.P., Jafri H.,
RA Rashid Y., Banin E., Strom T.M., Farber D.B., Sharon D., Blobel C.P.,
RA Pugh E.N. Jr., Pierce E.A., Inglehearn C.F.;
RT "Loss of the metalloprotease ADAM9 leads to cone-rod dystrophy in humans
RT and retinal degeneration in mice.";
RL Am. J. Hum. Genet. 84:683-691(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-758 AND THR-761, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: Cleaves and releases a number of molecules with important
CC roles in tumorigenesis and angiogenesis, such as TEK, KDR, EPHB4, CD40,
CC VCAM1 and CDH5. May mediate cell-cell, cell-matrix interactions and
CC regulate the motility of cells via interactions with integrins.
CC {ECO:0000250|UniProtKB:Q61072}.
CC -!- FUNCTION: [Isoform 2]: May act as alpha-secretase for amyloid precursor
CC protein (APP). {ECO:0000269|PubMed:12054541}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000305};
CC -!- ACTIVITY REGULATION: Synthesized as an inactive form which is
CC proteolytically cleaved to generate an active enzyme. Processing at the
CC upstream site is particularly important for activation of the
CC proenzyme, whereas processing at the boundary between the pro-domain
CC and the catalytic domain does not appear to be essential. Inhibited by
CC hydroxamic acid-based inhibitors. {ECO:0000250|UniProtKB:Q61072}.
CC -!- SUBUNIT: Interacts with SH3GL2 and SNX9 through its cytoplasmic tail
CC (PubMed:10531379). Interacts with ITGA6. {ECO:0000250|UniProtKB:Q61072,
CC ECO:0000269|PubMed:10531379}.
CC -!- INTERACTION:
CC Q13443; Q9UI95: MAD2L2; NbExp=3; IntAct=EBI-77903, EBI-77889;
CC Q13443; Q9UKS6: PACSIN3; NbExp=2; IntAct=EBI-77903, EBI-77926;
CC Q13443; Q99962: SH3GL2; NbExp=2; IntAct=EBI-77903, EBI-77938;
CC Q13443; Q96RF0: SNX18; NbExp=2; IntAct=EBI-77903, EBI-298169;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane
CC {ECO:0000269|PubMed:8647900}; Single-pass type I membrane protein
CC {ECO:0000255}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Secreted
CC {ECO:0000269|PubMed:12054541}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q13443-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q13443-2; Sequence=VSP_011057, VSP_011058;
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in chondrocytes.
CC Isoform 2 is highly expressed in liver and heart.
CC {ECO:0000269|PubMed:12054541, ECO:0000269|PubMed:7584026,
CC ECO:0000269|PubMed:8647900, ECO:0000269|PubMed:9016778}.
CC -!- PTM: Proteolytically cleaved in the trans-Golgi network before it
CC reaches the plasma membrane to generate a mature protein. The removal
CC of the pro-domain occurs via cleavage at two different sites. Processed
CC most likely by a pro-protein convertase such as furin, at the boundary
CC between the pro-domain and the catalytic domain. An additional upstream
CC cleavage pro-protein convertase site (Arg-56/Glu-57) has an important
CC role in the activation of ADAM9. {ECO:0000250|UniProtKB:Q61072}.
CC -!- PTM: Phosphorylation is induced in vitro by phorbol-12-myristate-13-
CC acetate (PMA). {ECO:0000250|UniProtKB:Q61072}.
CC -!- DISEASE: Cone-rod dystrophy 9 (CORD9) [MIM:612775]: An inherited
CC retinal dystrophy characterized by retinal pigment deposits visible on
CC fundus examination, predominantly in the macular region, and initial
CC loss of cone photoreceptors followed by rod degeneration. This leads to
CC decreased visual acuity and sensitivity in the central visual field,
CC followed by loss of peripheral vision. Severe loss of vision occurs
CC earlier than in retinitis pigmentosa, due to cone photoreceptors
CC degenerating at a higher rate than rod photoreceptors.
CC {ECO:0000269|PubMed:19409519}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- CAUTION: Has sometimes been referred to as ADAM-12. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/ADAM9ID573ch8p11.html";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U41766; AAC50403.1; -; mRNA.
DR EMBL; AF495383; AAM49575.1; -; mRNA.
DR EMBL; D14665; BAA03499.2; -; mRNA.
DR EMBL; CH471080; EAW63284.1; -; Genomic_DNA.
DR EMBL; BC143923; AAI43924.1; -; mRNA.
DR CCDS; CCDS6112.1; -. [Q13443-1]
DR PIR; JC7850; JC7850.
DR PIR; S71949; S71949.
DR RefSeq; NP_003807.1; NM_003816.2. [Q13443-1]
DR AlphaFoldDB; Q13443; -.
DR SMR; Q13443; -.
DR BioGRID; 114290; 129.
DR CORUM; Q13443; -.
DR IntAct; Q13443; 37.
DR MINT; Q13443; -.
DR STRING; 9606.ENSP00000419446; -.
DR BindingDB; Q13443; -.
DR ChEMBL; CHEMBL5982; -.
DR DrugBank; DB05033; INCB7839.
DR DrugCentral; Q13443; -.
DR GuidetoPHARMACOLOGY; 1657; -.
DR MEROPS; M12.209; -.
DR GlyConnect; 1181; 6 N-Linked glycans (1 site).
DR GlyGen; Q13443; 6 sites, 6 N-linked glycans (1 site).
DR iPTMnet; Q13443; -.
DR PhosphoSitePlus; Q13443; -.
DR BioMuta; ADAM9; -.
DR DMDM; 24211441; -.
DR EPD; Q13443; -.
DR jPOST; Q13443; -.
DR MassIVE; Q13443; -.
DR MaxQB; Q13443; -.
DR PaxDb; Q13443; -.
DR PeptideAtlas; Q13443; -.
DR PRIDE; Q13443; -.
DR ProteomicsDB; 59440; -. [Q13443-1]
DR ProteomicsDB; 59441; -. [Q13443-2]
DR ABCD; Q13443; 25 sequenced antibodies.
DR Antibodypedia; 1281; 354 antibodies from 34 providers.
DR DNASU; 8754; -.
DR Ensembl; ENST00000379917.7; ENSP00000369249.3; ENSG00000168615.13. [Q13443-2]
DR Ensembl; ENST00000487273.7; ENSP00000419446.2; ENSG00000168615.13. [Q13443-1]
DR GeneID; 8754; -.
DR KEGG; hsa:8754; -.
DR MANE-Select; ENST00000487273.7; ENSP00000419446.2; NM_003816.3; NP_003807.1.
DR UCSC; uc003xmr.4; human. [Q13443-1]
DR CTD; 8754; -.
DR DisGeNET; 8754; -.
DR GeneCards; ADAM9; -.
DR HGNC; HGNC:216; ADAM9.
DR HPA; ENSG00000168615; Low tissue specificity.
DR MalaCards; ADAM9; -.
DR MIM; 602713; gene.
DR MIM; 612775; phenotype.
DR neXtProt; NX_Q13443; -.
DR OpenTargets; ENSG00000168615; -.
DR Orphanet; 1872; Cone rod dystrophy.
DR PharmGKB; PA24534; -.
DR VEuPathDB; HostDB:ENSG00000168615; -.
DR eggNOG; KOG3607; Eukaryota.
DR GeneTree; ENSGT00940000156239; -.
DR HOGENOM; CLU_012714_4_1_1; -.
DR InParanoid; Q13443; -.
DR OrthoDB; 162519at2759; -.
DR PhylomeDB; Q13443; -.
DR TreeFam; TF314733; -.
DR BRENDA; 3.4.24.B9; 2681.
DR PathwayCommons; Q13443; -.
DR Reactome; R-HSA-1442490; Collagen degradation.
DR SignaLink; Q13443; -.
DR SIGNOR; Q13443; -.
DR BioGRID-ORCS; 8754; 9 hits in 1088 CRISPR screens.
DR ChiTaRS; ADAM9; human.
DR GeneWiki; ADAM9; -.
DR GenomeRNAi; 8754; -.
DR Pharos; Q13443; Tchem.
DR PRO; PR:Q13443; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q13443; protein.
DR Bgee; ENSG00000168615; Expressed in stromal cell of endometrium and 141 other tissues.
DR ExpressionAtlas; Q13443; baseline and differential.
DR Genevisible; Q13443; HS.
DR GO; GO:0009986; C:cell surface; ISS:BHF-UCL.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031233; C:intrinsic component of external side of plasma membrane; ISS:BHF-UCL.
DR GO; GO:0005518; F:collagen binding; IMP:BHF-UCL.
DR GO; GO:0005178; F:integrin binding; IDA:BHF-UCL.
DR GO; GO:0043236; F:laminin binding; IMP:BHF-UCL.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IDA:ARUK-UCL.
DR GO; GO:1902945; F:metalloendopeptidase activity involved in amyloid precursor protein catabolic process; IDA:ARUK-UCL.
DR GO; GO:0008237; F:metallopeptidase activity; IMP:BHF-UCL.
DR GO; GO:0005080; F:protein kinase C binding; ISS:BHF-UCL.
DR GO; GO:0017124; F:SH3 domain binding; IPI:BHF-UCL.
DR GO; GO:0042987; P:amyloid precursor protein catabolic process; IDA:ARUK-UCL.
DR GO; GO:0007155; P:cell adhesion; IMP:BHF-UCL.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; IMP:BHF-UCL.
DR GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR GO; GO:0033631; P:cell-cell adhesion mediated by integrin; IEP:BHF-UCL.
DR GO; GO:0007160; P:cell-matrix adhesion; IMP:BHF-UCL.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IMP:BHF-UCL.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IC:BHF-UCL.
DR GO; GO:0030216; P:keratinocyte differentiation; IEP:BHF-UCL.
DR GO; GO:0006509; P:membrane protein ectodomain proteolysis; IDA:BHF-UCL.
DR GO; GO:0031293; P:membrane protein intracellular domain proteolysis; IMP:ARUK-UCL.
DR GO; GO:0042117; P:monocyte activation; IMP:BHF-UCL.
DR GO; GO:0033630; P:positive regulation of cell adhesion mediated by integrin; IMP:BHF-UCL.
DR GO; GO:0030335; P:positive regulation of cell migration; IDA:ARUK-UCL.
DR GO; GO:0051549; P:positive regulation of keratinocyte migration; IMP:BHF-UCL.
DR GO; GO:0034241; P:positive regulation of macrophage fusion; IMP:BHF-UCL.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; IDA:BHF-UCL.
DR GO; GO:0051044; P:positive regulation of membrane protein ectodomain proteolysis; ISS:BHF-UCL.
DR GO; GO:0050714; P:positive regulation of protein secretion; IDA:BHF-UCL.
DR GO; GO:0016485; P:protein processing; IDA:ARUK-UCL.
DR GO; GO:0051592; P:response to calcium ion; IMP:BHF-UCL.
DR GO; GO:0051384; P:response to glucocorticoid; ISS:BHF-UCL.
DR GO; GO:0042542; P:response to hydrogen peroxide; IMP:BHF-UCL.
DR GO; GO:0010042; P:response to manganese ion; IMP:BHF-UCL.
DR GO; GO:0034612; P:response to tumor necrosis factor; IDA:BHF-UCL.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IMP:BHF-UCL.
DR CDD; cd04269; ZnMc_adamalysin_II_like; 1.
DR Gene3D; 3.40.390.10; -; 1.
DR Gene3D; 4.10.70.10; -; 1.
DR InterPro; IPR006586; ADAM_Cys-rich.
DR InterPro; IPR018358; Disintegrin_CS.
DR InterPro; IPR001762; Disintegrin_dom.
DR InterPro; IPR036436; Disintegrin_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR002870; Peptidase_M12B_N.
DR InterPro; IPR034027; Reprolysin_adamalysin.
DR Pfam; PF08516; ADAM_CR; 1.
DR Pfam; PF00200; Disintegrin; 1.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR SMART; SM00608; ACR; 1.
DR SMART; SM00050; DISIN; 1.
DR SUPFAM; SSF57552; SSF57552; 1.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS00427; DISINTEGRIN_1; 1.
DR PROSITE; PS50214; DISINTEGRIN_2; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cone-rod dystrophy; Disulfide bond;
KW Glycoprotein; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW Phosphoprotein; Protease; Reference proteome; Secreted; Signal;
KW Transmembrane; Transmembrane helix; Zinc.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..819
FT /note="Disintegrin and metalloproteinase domain-containing
FT protein 9"
FT /id="PRO_0000029062"
FT TOPO_DOM 29..697
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 698..718
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 719..819
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 212..406
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 414..501
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DOMAIN 644..698
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 734..763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 780..819
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 738..754
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 348
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 347
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 351
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 357
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT SITE 56..57
FT /note="Cleavage"
FT /evidence="ECO:0000250|UniProtKB:Q61072"
FT SITE 205..206
FT /note="Cleavage; by furin-like protease"
FT /evidence="ECO:0000250|UniProtKB:Q61072"
FT MOD_RES 758
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 761
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 154
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 381
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 487
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 322..401
FT /evidence="ECO:0000250"
FT DISULFID 363..385
FT /evidence="ECO:0000250"
FT DISULFID 365..370
FT /evidence="ECO:0000250"
FT DISULFID 473..493
FT /evidence="ECO:0000250"
FT DISULFID 644..656
FT /evidence="ECO:0000250"
FT DISULFID 650..662
FT /evidence="ECO:0000250"
FT DISULFID 664..673
FT /evidence="ECO:0000250"
FT VAR_SEQ 655
FT /note="V -> K (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12054541,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_011057"
FT VAR_SEQ 656..819
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12054541,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_011058"
FT CONFLICT 1..118
FT /note="Missing (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 117
FT /note="R -> Q (in Ref. 4; BAA03499)"
FT /evidence="ECO:0000305"
FT CONFLICT 119..135
FT /note="YVEGVHNSSIALSDCFG -> MWREFIIHPLLLATVLD (in Ref. 2;
FT no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 154
FT /note="N -> M (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 566
FT /note="G -> GLSLKFHAPFLSTMLQEAVRQTGTYLGGSVCCMKSDCRIVTLVK
FT (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 713..735
FT /note="AIFIFIKRDQLWRSYFRKKRSQT -> DYFYLHQEGSTVEKLLQKEEITN
FT (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 736..819
FT /note="Missing (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 819 AA; 90556 MW; BC186641833137FF CRC64;
MGSGARFPSG TLRVRWLLLL GLVGPVLGAA RPGFQQTSHL SSYEIITPWR LTRERREAPR
PYSKQVSYVI QAEGKEHIIH LERNKDLLPE DFVVYTYNKE GTLITDHPNI QNHCHYRGYV
EGVHNSSIAL SDCFGLRGLL HLENASYGIE PLQNSSHFEH IIYRMDDVYK EPLKCGVSNK
DIEKETAKDE EEEPPSMTQL LRRRRAVLPQ TRYVELFIVV DKERYDMMGR NQTAVREEMI
LLANYLDSMY IMLNIRIVLV GLEIWTNGNL INIVGGAGDV LGNFVQWREK FLITRRRHDS
AQLVLKKGFG GTAGMAFVGT VCSRSHAGGI NVFGQITVET FASIVAHELG HNLGMNHDDG
RDCSCGAKSC IMNSGASGSR NFSSCSAEDF EKLTLNKGGN CLLNIPKPDE AYSAPSCGNK
LVDAGEECDC GTPKECELDP CCEGSTCKLK SFAECAYGDC CKDCRFLPGG TLCRGKTSEC
DVPEYCNGSS QFCQPDVFIQ NGYPCQNNKA YCYNGMCQYY DAQCQVIFGS KAKAAPKDCF
IEVNSKGDRF GNCGFSGNEY KKCATGNALC GKLQCENVQE IPVFGIVPAI IQTPSRGTKC
WGVDFQLGSD VPDPGMVNEG TKCGAGKICR NFQCVDASVL NYDCDVQKKC HGHGVCNSNK
NCHCENGWAP PNCETKGYGG SVDSGPTYNE MNTALRDGLL VFFFLIVPLI VCAIFIFIKR
DQLWRSYFRK KRSQTYESDG KNQANPSRQP GSVPRHVSPV TPPREVPIYA NRFAVPTYAA
KQPQQFPSRP PPPQPKVSSQ GNLIPARPAP APPLYSSLT
