ADA33_HUMAN
ID ADA33_HUMAN Reviewed; 813 AA.
AC Q9BZ11; A0A1K6; Q5JT75; Q5JT76; Q8N0W6;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-MAR-2002, sequence version 2.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Disintegrin and metalloproteinase domain-containing protein 33;
DE Short=ADAM 33;
DE EC=3.4.24.-;
DE Flags: Precursor;
GN Name=ADAM33; Synonyms=C20orf153; ORFNames=UNQ873/PRO1891;
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] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=11814695; DOI=10.1016/s0378-1119(01)00818-6;
RA Yoshinaka T., Nishii K., Yamada K., Sawada H., Nishiwaki E., Smith K.,
RA Yoshino K., Ishiguro H., Higashiyama S.;
RT "Identification and characterization of novel mouse and human ADAM33s with
RT potential metalloprotease activity.";
RL Gene 282:227-236(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), AND INVOLVEMENT IN
RP ASTHMA.
RC TISSUE=Uterus;
RX PubMed=12110844; DOI=10.1038/nature00878;
RA Van Eerdewegh P., Little R.D., Dupuis J., Del Mastro R.G., Falls K.,
RA Simon J., Torrey D., Pandit S., McKenny J., Braunschweiger K., Walsh A.,
RA Liu Z., Hayward B., Folz C., Manning S.P., Bawa A., Saracino L.,
RA Thackston M., Benchekroun Y., Capparell N., Wang M., Adair R., Feng Y.,
RA Dubois J., FitzGerald M.G., Huang H., Gibson R., Allen K.M., Pedan A.,
RA Danzig M.R., Umland S.P., Egan R.W., Cuss F.M., Rorke S., Clough J.B.,
RA Holloway J.W., Holgate S.T., Keith T.P.;
RT "Association of the ADAM33 gene with asthma and bronchial
RT hyperresponsiveness.";
RL Nature 418:426-430(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SER-109; ALA-178; MET-272;
RP ILE-316; SER-336; SER-365; GLU-441; ARG-515; HIS-612; ILE-710; GLY-739;
RP TYR-742; THR-764 AND SER-774.
RG NIEHS SNPs program;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [6]
RP INVOLVEMENT IN SUSCEPTIBILITY TO ASTHMA.
RX PubMed=16773130; DOI=10.1038/sj.ejhg.5201662;
RA Kedda M.A., Duffy D.L., Bradley B., O'Hehir R.E., Thompson P.J.;
RT "ADAM33 haplotypes are associated with asthma in a large Australian
RT population.";
RL Eur. J. Hum. Genet. 14:1027-1036(2006).
RN [7]
RP INVOLVEMENT IN SUSCEPTIBILITY TO ASTHMA.
RX PubMed=19237393; DOI=10.1136/thx.2008.102053;
RA Blakey J.D., Sayers I., Ring S.M., Strachan D.P., Hall I.P.;
RT "Positionally cloned asthma susceptibility gene polymorphisms and disease
RT risk in the British 1958 Birth Cohort.";
RL Thorax 64:381-387(2009).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.58 ANGSTROMS) OF 204-410 IN COMPLEX WITH
RP METALLOPROTEASE INHIBITOR MARIMASTAT AND ZINC, X-RAY CRYSTALLOGRAPHY (1.85
RP ANGSTROMS) OF 204-410, AND COFACTOR.
RX PubMed=14659745; DOI=10.1016/j.jmb.2003.10.037;
RA Orth P., Reichert P., Wang W., Prosise W.W., Yarosh-Tomaine T., Hammond G.,
RA Ingram R.N., Xiao L., Mirza U.A., Zou J., Strickland C., Taremi S.S.,
RA Le H.V., Madison V.;
RT "Crystal structure of the catalytic domain of human ADAM33.";
RL J. Mol. Biol. 335:129-137(2004).
RN [9]
RP VARIANT VAL-305.
RX PubMed=21618342; DOI=10.1002/humu.21477;
RA Wei X., Moncada-Pazos A., Cal S., Soria-Valles C., Gartner J., Rudloff U.,
RA Lin J.C., Rosenberg S.A., Lopez-Otin C., Samuels Y.;
RT "Analysis of the disintegrin-metalloproteinases family reveals ADAM29 and
RT ADAM7 are often mutated in melanoma.";
RL Hum. Mutat. 32:E2148-E2175(2011).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:14659745};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:14659745};
CC -!- INTERACTION:
CC Q9BZ11-2; Q9BXN2: CLEC7A; NbExp=3; IntAct=EBI-10303054, EBI-3939278;
CC Q9BZ11-2; Q9BRI3: SLC30A2; NbExp=3; IntAct=EBI-10303054, EBI-8644112;
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=Q9BZ11-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BZ11-2; Sequence=VSP_005495;
CC Name=3;
CC IsoId=Q9BZ11-3; Sequence=VSP_015421, VSP_005495;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues, except liver, with high
CC expression in placenta, lung, spleen and veins.
CC {ECO:0000269|PubMed:11814695}.
CC -!- DOMAIN: The conserved cysteine present in the cysteine-switch motif
CC binds the catalytic zinc ion, thus inhibiting the enzyme. The
CC dissociation of the cysteine from the zinc ion upon the activation-
CC peptide release activates the enzyme.
CC -!- PTM: The precursor is cleaved by a furin endopeptidase. {ECO:0000250}.
CC -!- DISEASE: Asthma (ASTHMA) [MIM:600807]: The most common chronic disease
CC affecting children and young adults. It is a complex genetic disorder
CC with a heterogeneous phenotype, largely attributed to the interactions
CC among many genes and between these genes and the environment. It is
CC characterized by recurrent attacks of paroxysmal dyspnea, with wheezing
CC due to spasmodic contraction of the bronchi.
CC {ECO:0000269|PubMed:12110844, ECO:0000269|PubMed:16773130,
CC ECO:0000269|PubMed:19237393}. Note=Disease susceptibility is associated
CC with variants affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: [Isoform 3]: By similarity with mouse isoform.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/adam33/";
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DR EMBL; AB055891; BAB83092.1; -; mRNA.
DR EMBL; AF466287; AAM80482.1; -; mRNA.
DR EMBL; AF466288; AAM80483.1; -; Genomic_DNA.
DR EMBL; AY358314; AAQ88680.1; -; mRNA.
DR EMBL; DQ995342; ABI97387.1; -; Genomic_DNA.
DR EMBL; AL109804; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL356755; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS13058.1; -. [Q9BZ11-1]
DR RefSeq; NP_001269376.1; NM_001282447.2.
DR RefSeq; NP_079496.1; NM_025220.4. [Q9BZ11-1]
DR RefSeq; NP_694882.1; NM_153202.3. [Q9BZ11-2]
DR PDB; 1R54; X-ray; 1.85 A; A=204-409.
DR PDB; 1R55; X-ray; 1.58 A; A=204-409.
DR PDBsum; 1R54; -.
DR PDBsum; 1R55; -.
DR AlphaFoldDB; Q9BZ11; -.
DR SMR; Q9BZ11; -.
DR BioGRID; 123243; 93.
DR IntAct; Q9BZ11; 40.
DR STRING; 9606.ENSP00000348912; -.
DR BindingDB; Q9BZ11; -.
DR ChEMBL; CHEMBL6121; -.
DR GuidetoPHARMACOLOGY; 1673; -.
DR MEROPS; M12.244; -.
DR GlyGen; Q9BZ11; 5 sites.
DR iPTMnet; Q9BZ11; -.
DR PhosphoSitePlus; Q9BZ11; -.
DR BioMuta; ADAM33; -.
DR DMDM; 20137458; -.
DR jPOST; Q9BZ11; -.
DR MassIVE; Q9BZ11; -.
DR PaxDb; Q9BZ11; -.
DR PeptideAtlas; Q9BZ11; -.
DR PRIDE; Q9BZ11; -.
DR ProteomicsDB; 79748; -. [Q9BZ11-1]
DR ProteomicsDB; 79749; -. [Q9BZ11-2]
DR Antibodypedia; 7461; 195 antibodies from 34 providers.
DR DNASU; 80332; -.
DR Ensembl; ENST00000350009.6; ENSP00000322550.5; ENSG00000149451.19. [Q9BZ11-2]
DR Ensembl; ENST00000356518.7; ENSP00000348912.3; ENSG00000149451.19. [Q9BZ11-1]
DR GeneID; 80332; -.
DR KEGG; hsa:80332; -.
DR MANE-Select; ENST00000356518.7; ENSP00000348912.3; NM_025220.5; NP_079496.1.
DR UCSC; uc002wit.5; human. [Q9BZ11-1]
DR CTD; 80332; -.
DR DisGeNET; 80332; -.
DR GeneCards; ADAM33; -.
DR HGNC; HGNC:15478; ADAM33.
DR HPA; ENSG00000149451; Tissue enhanced (cervix).
DR MIM; 600807; phenotype.
DR MIM; 607114; gene.
DR neXtProt; NX_Q9BZ11; -.
DR OpenTargets; ENSG00000149451; -.
DR PharmGKB; PA24526; -.
DR VEuPathDB; HostDB:ENSG00000149451; -.
DR eggNOG; KOG3607; Eukaryota.
DR GeneTree; ENSGT00940000158971; -.
DR HOGENOM; CLU_012714_7_2_1; -.
DR InParanoid; Q9BZ11; -.
DR OMA; ETHYTTD; -.
DR OrthoDB; 162519at2759; -.
DR PhylomeDB; Q9BZ11; -.
DR TreeFam; TF314733; -.
DR PathwayCommons; Q9BZ11; -.
DR SignaLink; Q9BZ11; -.
DR BioGRID-ORCS; 80332; 20 hits in 1075 CRISPR screens.
DR EvolutionaryTrace; Q9BZ11; -.
DR GeneWiki; ADAM33; -.
DR GenomeRNAi; 80332; -.
DR Pharos; Q9BZ11; Tchem.
DR PRO; PR:Q9BZ11; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q9BZ11; protein.
DR Bgee; ENSG00000149451; Expressed in endocervix and 172 other tissues.
DR ExpressionAtlas; Q9BZ11; baseline and differential.
DR Genevisible; Q9BZ11; HS.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0004222; F:metalloendopeptidase activity; NAS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; NAS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; NAS:UniProtKB.
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; Asthma;
KW Cleavage on pair of basic residues; Disulfide bond; EGF-like domain;
KW Glycoprotein; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW Protease; Reference proteome; Signal; Transmembrane; Transmembrane helix;
KW Zinc; Zymogen.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT PROPEP 30..203
FT /evidence="ECO:0000250"
FT /id="PRO_0000029142"
FT CHAIN 204..813
FT /note="Disintegrin and metalloproteinase domain-containing
FT protein 33"
FT /id="PRO_0000029143"
FT TOPO_DOM 30..701
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 702..722
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 723..813
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 210..409
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 417..503
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DOMAIN 649..681
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 184..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 746..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 131..138
FT /note="Cysteine switch"
FT /evidence="ECO:0000250"
FT COMPBIAS 746..760
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 346
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 133
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /note="in inhibited form"
FT /evidence="ECO:0000250"
FT BINDING 345
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:14659745"
FT BINDING 349
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:14659745"
FT BINDING 355
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:14659745"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 276
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 448
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 320..404
FT /evidence="ECO:0000269|PubMed:14659745"
FT DISULFID 360..388
FT /evidence="ECO:0000269|PubMed:14659745"
FT DISULFID 361..371
FT /evidence="ECO:0000269|PubMed:14659745"
FT DISULFID 475..495
FT /evidence="ECO:0000250"
FT DISULFID 653..663
FT /evidence="ECO:0000250"
FT DISULFID 657..669
FT /evidence="ECO:0000250"
FT DISULFID 671..680
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..478
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_015421"
FT VAR_SEQ 636..661
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:11814695"
FT /id="VSP_005495"
FT VARIANT 109
FT /note="N -> S (in dbSNP:rs41467948)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_030512"
FT VARIANT 178
FT /note="T -> A (in dbSNP:rs3918392)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_029143"
FT VARIANT 272
FT /note="T -> M (in dbSNP:rs41534847)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_030513"
FT VARIANT 305
FT /note="A -> V (in a cutaneous metastatic melanoma sample;
FT somatic mutation; dbSNP:rs1169229302)"
FT /evidence="ECO:0000269|PubMed:21618342"
FT /id="VAR_066337"
FT VARIANT 316
FT /note="V -> I (in dbSNP:rs41459049)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_030514"
FT VARIANT 336
FT /note="P -> S (in dbSNP:rs41483049)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_030515"
FT VARIANT 365
FT /note="A -> S (in dbSNP:rs41419248)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_030516"
FT VARIANT 441
FT /note="D -> E (in dbSNP:rs41382144)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_030517"
FT VARIANT 515
FT /note="W -> R (in dbSNP:rs615436)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_030518"
FT VARIANT 612
FT /note="L -> H (in dbSNP:rs41453444)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_030519"
FT VARIANT 710
FT /note="V -> I (in dbSNP:rs3918396)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_030520"
FT VARIANT 739
FT /note="C -> G (in dbSNP:rs41434648)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_030521"
FT VARIANT 742
FT /note="D -> Y (in dbSNP:rs41462450)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_030522"
FT VARIANT 764
FT /note="M -> T (in dbSNP:rs2280091)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_021847"
FT VARIANT 774
FT /note="P -> S (in dbSNP:rs2280090)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_029144"
FT CONFLICT 802
FT /note="Missing (in Ref. 2; AAM80482/AAM80483)"
FT /evidence="ECO:0000305"
FT STRAND 210..218
FT /evidence="ECO:0007829|PDB:1R55"
FT HELIX 220..225
FT /evidence="ECO:0007829|PDB:1R55"
FT TURN 226..228
FT /evidence="ECO:0007829|PDB:1R55"
FT HELIX 230..248
FT /evidence="ECO:0007829|PDB:1R55"
FT HELIX 249..251
FT /evidence="ECO:0007829|PDB:1R55"
FT STRAND 253..262
FT /evidence="ECO:0007829|PDB:1R55"
FT STRAND 264..266
FT /evidence="ECO:0007829|PDB:1R55"
FT HELIX 275..292
FT /evidence="ECO:0007829|PDB:1R55"
FT STRAND 296..303
FT /evidence="ECO:0007829|PDB:1R55"
FT HELIX 307..309
FT /evidence="ECO:0007829|PDB:1R55"
FT TURN 322..324
FT /evidence="ECO:0007829|PDB:1R55"
FT STRAND 326..330
FT /evidence="ECO:0007829|PDB:1R55"
FT STRAND 333..335
FT /evidence="ECO:0007829|PDB:1R55"
FT HELIX 336..350
FT /evidence="ECO:0007829|PDB:1R55"
FT HELIX 366..368
FT /evidence="ECO:0007829|PDB:1R55"
FT HELIX 387..398
FT /evidence="ECO:0007829|PDB:1R55"
FT TURN 399..402
FT /evidence="ECO:0007829|PDB:1R55"
FT HELIX 403..406
FT /evidence="ECO:0007829|PDB:1R55"
SQ SEQUENCE 813 AA; 87739 MW; 90713A99668D5569 CRC64;
MGWRPRRARG TPLLLLLLLL LLWPVPGAGV LQGHIPGQPV TPHWVLDGQP WRTVSLEEPV
SKPDMGLVAL EAEGQELLLE LEKNHRLLAP GYIETHYGPD GQPVVLAPNH TDHCHYQGRV
RGFPDSWVVL CTCSGMSGLI TLSRNASYYL RPWPPRGSKD FSTHEIFRME QLLTWKGTCG
HRDPGNKAGM TSLPGGPQSR GRREARRTRK YLELYIVADH TLFLTRHRNL NHTKQRLLEV
ANYVDQLLRT LDIQVALTGL EVWTERDRSR VTQDANATLW AFLQWRRGLW AQRPHDSAQL
LTGRAFQGAT VGLAPVEGMC RAESSGGVST DHSELPIGAA ATMAHEIGHS LGLSHDPDGC
CVEAAAESGG CVMAAATGHP FPRVFSACSR RQLRAFFRKG GGACLSNAPD PGLPVPPALC
GNGFVEAGEE CDCGPGQECR DLCCFAHNCS LRPGAQCAHG DCCVRCLLKP AGALCRQAMG
DCDLPEFCTG TSSHCPPDVY LLDGSPCARG SGYCWDGACP TLEQQCQQLW GPGSHPAPEA
CFQVVNSAGD AHGNCGQDSE GHFLPCAGRD ALCGKLQCQG GKPSLLAPHM VPVDSTVHLD
GQEVTCRGAL ALPSAQLDLL GLGLVEPGTQ CGPRMVCQSR RCRKNAFQEL QRCLTACHSH
GVCNSNHNCH CAPGWAPPFC DKPGFGGSMD SGPVQAENHD TFLLAMLLSV LLPLLPGAGL
AWCCYRLPGA HLQRCSWGCR RDPACSGPKD GPHRDHPLGG VHPMELGPTA TGQPWPLDPE
NSHEPSSHPE KPLPAVSPDP QADQVQMPRS CLW
