ADAM8_HUMAN
ID ADAM8_HUMAN Reviewed; 824 AA.
AC P78325; B4DVM6; H0YL36; H0YLR0; H0YN39;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Disintegrin and metalloproteinase domain-containing protein 8;
DE Short=ADAM 8;
DE EC=3.4.24.-;
DE AltName: Full=Cell surface antigen MS2;
DE AltName: CD_antigen=CD156a;
DE Flags: Precursor;
GN Name=ADAM8; Synonyms=MS2;
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), AND VARIANT ARG-35.
RC TISSUE=Blood;
RX PubMed=9126482; DOI=10.1006/geno.1997.4607;
RA Yoshiyama K., Higuchi Y., Kataoka M., Matsuura K., Yamamoto S.;
RT "CD156 (human ADAM8): expression, primary amino acid sequence, and gene
RT location.";
RL Genomics 41:56-62(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT LEU-657.
RC TISSUE=Spleen;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT ARG-35.
RC TISSUE=Pancreatic cancer;
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 [5]
RP INTERACTION WITH FST3.
RX PubMed=15574124; DOI=10.1042/bc20040506;
RA Bartholin L., Destaing O., Forissier S., Martel S., Maguer-Satta V.,
RA Jurdic P., Rimokh R.;
RT "FLRG, a new ADAM12-associated protein, modulates osteoclast
RT differentiation.";
RL Biol. Cell 97:577-588(2005).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 196-403 IN COMPLEX WITH INHIBITOR
RP AND ZINC IONS, AND COFACTOR.
RX PubMed=22684055; DOI=10.1107/s1744309112015618;
RA Hall T., Shieh H.S., Day J.E., Caspers N., Chrencik J.E., Williams J.M.,
RA Pegg L.E., Pauley A.M., Moon A.F., Krahn J.M., Fischer D.H., Kiefer J.R.,
RA Tomasselli A.G., Zack M.D.;
RT "Structure of human ADAM-8 catalytic domain complexed with batimastat.";
RL Acta Crystallogr. F 68:616-621(2012).
CC -!- FUNCTION: Possible involvement in extravasation of leukocytes.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:22684055};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:22684055};
CC -!- SUBUNIT: Interacts with FST3. {ECO:0000269|PubMed:15574124}.
CC -!- INTERACTION:
CC P78325; Q5T0N5: FNBP1L; NbExp=2; IntAct=EBI-2625954, EBI-714058;
CC P78325; P14598: NCF1; NbExp=2; IntAct=EBI-2625954, EBI-395044;
CC P78325; P42680: TEC; NbExp=2; IntAct=EBI-2625954, EBI-1383480;
CC P78325; Q15642: TRIP10; NbExp=2; IntAct=EBI-2625954, EBI-739936;
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P78325-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P78325-2; Sequence=VSP_046154, VSP_046155, VSP_046156,
CC VSP_046159;
CC Name=3;
CC IsoId=P78325-3; Sequence=VSP_046157, VSP_046158;
CC -!- TISSUE SPECIFICITY: Expressed on neutrophils and monocytes.
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DR EMBL; D26579; BAA05626.1; -; mRNA.
DR EMBL; AK301147; BAG62738.1; -; mRNA.
DR EMBL; AL592071; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC064500; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS31319.2; -. [P78325-1]
DR CCDS; CCDS58102.1; -. [P78325-2]
DR CCDS; CCDS58103.1; -. [P78325-3]
DR RefSeq; NP_001100.3; NM_001109.4. [P78325-1]
DR RefSeq; NP_001157961.1; NM_001164489.1. [P78325-3]
DR RefSeq; NP_001157962.1; NM_001164490.1. [P78325-2]
DR PDB; 4DD8; X-ray; 2.10 A; A/B/C/D=196-403.
DR PDBsum; 4DD8; -.
DR AlphaFoldDB; P78325; -.
DR SMR; P78325; -.
DR BioGRID; 106615; 3.
DR CORUM; P78325; -.
DR IntAct; P78325; 12.
DR STRING; 9606.ENSP00000453302; -.
DR BindingDB; P78325; -.
DR ChEMBL; CHEMBL5665; -.
DR GuidetoPHARMACOLOGY; 1656; -.
DR MEROPS; M12.208; -.
DR GlyConnect; 1996; 2 N-Linked glycans (1 site).
DR GlyGen; P78325; 4 sites, 2 N-linked glycans (1 site).
DR iPTMnet; P78325; -.
DR PhosphoSitePlus; P78325; -.
DR BioMuta; ADAM8; -.
DR DMDM; 408359955; -.
DR jPOST; P78325; -.
DR MassIVE; P78325; -.
DR MaxQB; P78325; -.
DR PaxDb; P78325; -.
DR PeptideAtlas; P78325; -.
DR PRIDE; P78325; -.
DR ProteomicsDB; 39834; -.
DR ProteomicsDB; 40029; -.
DR ProteomicsDB; 40447; -.
DR ProteomicsDB; 57567; -. [P78325-1]
DR ABCD; P78325; 19 sequenced antibodies.
DR Antibodypedia; 19390; 434 antibodies from 39 providers.
DR DNASU; 101; -.
DR Ensembl; ENST00000415217.7; ENSP00000453855.1; ENSG00000151651.16. [P78325-3]
DR Ensembl; ENST00000445355.8; ENSP00000453302.1; ENSG00000151651.16. [P78325-1]
DR Ensembl; ENST00000485491.6; ENSP00000453043.1; ENSG00000151651.16. [P78325-2]
DR GeneID; 101; -.
DR KEGG; hsa:101; -.
DR MANE-Select; ENST00000445355.8; ENSP00000453302.1; NM_001109.5; NP_001100.3.
DR UCSC; uc009ybi.4; human. [P78325-1]
DR CTD; 101; -.
DR DisGeNET; 101; -.
DR GeneCards; ADAM8; -.
DR HGNC; HGNC:215; ADAM8.
DR HPA; ENSG00000151651; Tissue enhanced (bone marrow, lymphoid tissue).
DR MIM; 602267; gene.
DR neXtProt; NX_P78325; -.
DR OpenTargets; ENSG00000151651; -.
DR VEuPathDB; HostDB:ENSG00000151651; -.
DR eggNOG; KOG3607; Eukaryota.
DR GeneTree; ENSGT00940000158585; -.
DR HOGENOM; CLU_012714_7_1_1; -.
DR InParanoid; P78325; -.
DR OMA; HGQDHCL; -.
DR OrthoDB; 162519at2759; -.
DR PhylomeDB; P78325; -.
DR TreeFam; TF314733; -.
DR PathwayCommons; P78325; -.
DR Reactome; R-HSA-1474228; Degradation of the extracellular matrix.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; P78325; -.
DR BioGRID-ORCS; 101; 6 hits in 1076 CRISPR screens.
DR ChiTaRS; ADAM8; human.
DR GeneWiki; ADAM8; -.
DR GenomeRNAi; 101; -.
DR Pharos; P78325; Tchem.
DR PRO; PR:P78325; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; P78325; protein.
DR Bgee; ENSG00000151651; Expressed in granulocyte and 116 other tissues.
DR ExpressionAtlas; P78325; baseline and differential.
DR Genevisible; P78325; HS.
DR GO; GO:0071133; C:alpha9-beta1 integrin-ADAM8 complex; ISS:BHF-UCL.
DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0032127; C:dense core granule membrane; IDA:BHF-UCL.
DR GO; GO:0101003; C:ficolin-1-rich granule membrane; TAS:Reactome.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:BHF-UCL.
DR GO; GO:0032010; C:phagolysosome; IDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR GO; GO:0002102; C:podosome; IDA:BHF-UCL.
DR GO; GO:0042581; C:specific granule; IDA:BHF-UCL.
DR GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
DR GO; GO:0070820; C:tertiary granule; IDA:BHF-UCL.
DR GO; GO:0070821; C:tertiary granule membrane; TAS:Reactome.
DR GO; GO:0005509; F:calcium ion binding; ISS:BHF-UCL.
DR GO; GO:0050839; F:cell adhesion molecule binding; IPI:BHF-UCL.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008237; F:metallopeptidase activity; IDA:BHF-UCL.
DR GO; GO:0043621; F:protein self-association; TAS:BHF-UCL.
DR GO; GO:0004252; F:serine-type endopeptidase activity; TAS:Reactome.
DR GO; GO:0008270; F:zinc ion binding; TAS:BHF-UCL.
DR GO; GO:0001525; P:angiogenesis; ISS:BHF-UCL.
DR GO; GO:0000902; P:cell morphogenesis; ISS:BHF-UCL.
DR GO; GO:0098609; P:cell-cell adhesion; IEA:Ensembl.
DR GO; GO:0071456; P:cellular response to hypoxia; IDA:BHF-UCL.
DR GO; GO:0022617; P:extracellular matrix disassembly; TAS:Reactome.
DR GO; GO:0006954; P:inflammatory response; IDA:BHF-UCL.
DR GO; GO:0002523; P:leukocyte migration involved in inflammatory response; ISS:BHF-UCL.
DR GO; GO:0048247; P:lymphocyte chemotaxis; ISS:BHF-UCL.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISS:BHF-UCL.
DR GO; GO:0002675; P:positive regulation of acute inflammatory response; ISS:BHF-UCL.
DR GO; GO:0045780; P:positive regulation of bone resorption; ISS:BHF-UCL.
DR GO; GO:0045785; P:positive regulation of cell adhesion; ISS:BHF-UCL.
DR GO; GO:0002693; P:positive regulation of cellular extravasation; IBA:GO_Central.
DR GO; GO:2000418; P:positive regulation of eosinophil migration; ISS:BHF-UCL.
DR GO; GO:2000415; P:positive regulation of fibronectin-dependent thymocyte migration; ISS:BHF-UCL.
DR GO; GO:0045089; P:positive regulation of innate immune response; ISS:BHF-UCL.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; ISS:BHF-UCL.
DR GO; GO:0051044; P:positive regulation of membrane protein ectodomain proteolysis; IDA:BHF-UCL.
DR GO; GO:2000391; P:positive regulation of neutrophil extravasation; IDA:BHF-UCL.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:BHF-UCL.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISS:BHF-UCL.
DR GO; GO:0010954; P:positive regulation of protein processing; NAS:BHF-UCL.
DR GO; GO:0050714; P:positive regulation of protein secretion; IC:BHF-UCL.
DR GO; GO:0033089; P:positive regulation of T cell differentiation in thymus; ISS:BHF-UCL.
DR GO; GO:0070245; P:positive regulation of thymocyte apoptotic process; ISS:BHF-UCL.
DR GO; GO:2000309; P:positive regulation of tumor necrosis factor (ligand) superfamily member 11 production; ISS:BHF-UCL.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0022407; P:regulation of cell-cell adhesion; IDA: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 PRINTS; PR00289; DISINTEGRIN.
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 3D-structure; Alternative splicing; Disulfide bond; EGF-like domain;
KW Glycoprotein; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW Protease; Reference proteome; Signal; Transmembrane; Transmembrane helix;
KW Zinc.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..824
FT /note="Disintegrin and metalloproteinase domain-containing
FT protein 8"
FT /id="PRO_0000029060"
FT TOPO_DOM 17..655
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 656..676
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 677..824
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 200..400
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 408..494
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DOMAIN 609..641
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 710..756
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 776..824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 777..791
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 335
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 334
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:22684055"
FT BINDING 338
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:22684055"
FT BINDING 344
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:22684055"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 436
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 612
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 310..395
FT /evidence="ECO:0000250"
FT DISULFID 351..379
FT /evidence="ECO:0000250"
FT DISULFID 353..362
FT /evidence="ECO:0000250"
FT DISULFID 435..457
FT /evidence="ECO:0000250|UniProtKB:Q10741"
FT DISULFID 448..454
FT /evidence="ECO:0000250|UniProtKB:Q10741"
FT DISULFID 466..486
FT /evidence="ECO:0000250|UniProtKB:Q10741"
FT DISULFID 473..503
FT /evidence="ECO:0000250|UniProtKB:Q10741"
FT DISULFID 498..508
FT /evidence="ECO:0000250|UniProtKB:Q10741"
FT DISULFID 566..613
FT /evidence="ECO:0000250|UniProtKB:Q10741"
FT DISULFID 613..623
FT /evidence="ECO:0000250"
FT DISULFID 617..629
FT /evidence="ECO:0000250"
FT DISULFID 631..640
FT /evidence="ECO:0000250"
FT VAR_SEQ 16..92
FT /note="AIAPSRPWALMEQYEVVLPWRLPGPRVRRALPSHLGLHPERVSYVLGATGHN
FT FTLHLRKNRDLLGSGYTETYTAANG -> GPAPREGELRPWGHRAQLHPPPAEEQGPAG
FT LRLHRDLYGCQWLRGDGAASRAGPLLLPGPRRGVPGLSRQPQHLCRP (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046154"
FT VAR_SEQ 93..131
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046155"
FT VAR_SEQ 596..621
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046156"
FT VAR_SEQ 650..742
FT /note="ASGSLPVFVVVVLVLLAVVLVTLAGIIVYRKARSRILSRNVAPKTTMGRSNP
FT LFHQAASRVPAKGGAPAPSRGPQELVPTTHPGQPARHPASS -> GCQPRAGQGRGSSP
FT IQGPPRAGPHHPPGPARPTPGLLGGSEEAAPCSSGHCVQPTLPSSCLHPAGTKAGHQAN
FT VRTPSAPSQTRGWCGQPWSS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_046157"
FT VAR_SEQ 743..824
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_046158"
FT VAR_SEQ 774..799
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046159"
FT VARIANT 35
FT /note="W -> R (in dbSNP:rs2275725)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:9126482"
FT /id="VAR_069144"
FT VARIANT 101
FT /note="G -> R (in dbSNP:rs11101675)"
FT /id="VAR_059760"
FT VARIANT 189
FT /note="R -> W (in dbSNP:rs45451297)"
FT /id="VAR_061735"
FT VARIANT 433
FT /note="R -> C (in dbSNP:rs12257830)"
FT /id="VAR_061736"
FT VARIANT 657
FT /note="F -> L (in dbSNP:rs2275720)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_069145"
FT VARIANT 775
FT /note="I -> T (in dbSNP:rs3008319)"
FT /id="VAR_061737"
FT CONFLICT 106
FT /note="F -> L (in Ref. 1; BAA05626)"
FT /evidence="ECO:0000305"
FT CONFLICT 372
FT /note="F -> L (in Ref. 2; BAG62738)"
FT /evidence="ECO:0000305"
FT CONFLICT 648
FT /note="H -> D (in Ref. 2; BAG62738)"
FT /evidence="ECO:0000305"
FT STRAND 200..208
FT /evidence="ECO:0007829|PDB:4DD8"
FT HELIX 210..216
FT /evidence="ECO:0007829|PDB:4DD8"
FT HELIX 219..237
FT /evidence="ECO:0007829|PDB:4DD8"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:4DD8"
FT STRAND 242..251
FT /evidence="ECO:0007829|PDB:4DD8"
FT HELIX 264..276
FT /evidence="ECO:0007829|PDB:4DD8"
FT TURN 279..281
FT /evidence="ECO:0007829|PDB:4DD8"
FT STRAND 286..292
FT /evidence="ECO:0007829|PDB:4DD8"
FT STRAND 302..304
FT /evidence="ECO:0007829|PDB:4DD8"
FT STRAND 315..319
FT /evidence="ECO:0007829|PDB:4DD8"
FT HELIX 325..339
FT /evidence="ECO:0007829|PDB:4DD8"
FT HELIX 345..347
FT /evidence="ECO:0007829|PDB:4DD8"
FT HELIX 378..387
FT /evidence="ECO:0007829|PDB:4DD8"
FT HELIX 391..396
FT /evidence="ECO:0007829|PDB:4DD8"
FT CONFLICT P78325-2:46
FT /note="L -> F (in Ref. 2; BAG62738)"
FT /evidence="ECO:0000305"
FT CONFLICT P78325-3:693
FT /note="A -> S (in Ref. 4; BC064500)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 824 AA; 88771 MW; CE3D31330E153DB8 CRC64;
MRGLGLWLLG AMMLPAIAPS RPWALMEQYE VVLPWRLPGP RVRRALPSHL GLHPERVSYV
LGATGHNFTL HLRKNRDLLG SGYTETYTAA NGSEVTEQPR GQDHCFYQGH VEGYPDSAAS
LSTCAGLRGF FQVGSDLHLI EPLDEGGEGG RHAVYQAEHL LQTAGTCGVS DDSLGSLLGP
RTAAVFRPRP GDSLPSRETR YVELYVVVDN AEFQMLGSEA AVRHRVLEVV NHVDKLYQKL
NFRVVLVGLE IWNSQDRFHV SPDPSVTLEN LLTWQARQRT RRHLHDNVQL ITGVDFTGTT
VGFARVSAMC SHSSGAVNQD HSKNPVGVAC TMAHEMGHNL GMDHDENVQG CRCQERFEAG
RCIMAGSIGS SFPRMFSDCS QAYLESFLER PQSVCLANAP DLSHLVGGPV CGNLFVERGE
QCDCGPPEDC RNRCCNSTTC QLAEGAQCAH GTCCQECKVK PAGELCRPKK DMCDLEEFCD
GRHPECPEDA FQENGTPCSG GYCYNGACPT LAQQCQAFWG PGGQAAEESC FSYDILPGCK
ASRYRADMCG VLQCKGGQQP LGRAICIVDV CHALTTEDGT AYEPVPEGTR CGPEKVCWKG
RCQDLHVYRS SNCSAQCHNH GVCNHKQECH CHAGWAPPHC AKLLTEVHAA SGSLPVFVVV
VLVLLAVVLV TLAGIIVYRK ARSRILSRNV APKTTMGRSN PLFHQAASRV PAKGGAPAPS
RGPQELVPTT HPGQPARHPA SSVALKRPPP APPVTVSSPP FPVPVYTRQA PKQVIKPTFA
PPVPPVKPGA GAANPGPAEG AVGPKVALKP PIQRKQGAGA PTAP
