ID   IRAK2_HUMAN             Reviewed;         625 AA.
AC   O43187; B4DQZ6; Q08AG6; Q5K546;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 2.
DT   27-MAR-2024, entry version 198.
DE   RecName: Full=Interleukin-1 receptor-associated kinase-like 2;
DE            Short=IRAK-2;
GN   Name=IRAK2;
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], AND VARIANT GLU-431.
RA   Rosati O., Martin M.U.;
RT   "Identification of Exon 13 and the 3'UTR region of human IRAK-2 and
RT   characterisation of the full length gene.";
RL   Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 MRNA].
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   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-590, FUNCTION, TISSUE SPECIFICITY,
RP   INTERACTION WITH TRAF6; MYD88 AND IL1R1, AND VARIANT GLU-431.
RC   TISSUE=Endothelial cell;
RX   PubMed=9374458; DOI=10.1126/science.278.5343.1612;
RA   Muzio M., Ni J., Feng P., Dixit V.M.;
RT   "IRAK (Pelle) family member IRAK-2 and MyD88 as proximal mediators of IL-1
RT   signaling.";
RL   Science 278:1612-1615(1997).
RN   [5]
RP   FUNCTION.
RX   PubMed=10383454; DOI=10.1074/jbc.274.27.19403;
RA   Wesche H., Gao X., Li X., Kirschning C.J., Stark G.R., Cao Z.;
RT   "IRAK-M is a novel member of the Pelle/interleukin-1 receptor-associated
RT   kinase (IRAK) family.";
RL   J. Biol. Chem. 274:19403-19410(1999).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-144, AND IDENTIFICATION BY
RP   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).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (3.40 ANGSTROMS) OF 2-112.
RX   PubMed=20485341; DOI=10.1038/nature09121;
RA   Lin S.-C., Lo Y.-C., Wu H.;
RT   "Helical assembly in the MyD88-IRAK4-IRAK2 complex in TLR/IL-1R
RT   signalling.";
RL   Nature 465:885-890(2010).
RN   [9]
RP   VARIANTS [LARGE SCALE ANALYSIS] GLN-43; TYR-47; VAL-99; THR-147; GLY-214;
RP   LEU-249; VAL-392; THR-421; GLU-431; VAL-439; ASN-469; ILE-503 AND TRP-566.
RX   PubMed=17344846; DOI=10.1038/nature05610;
RA   Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA   Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA   Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA   Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA   Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA   Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA   Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA   Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA   Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA   Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA   Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA   Futreal P.A., Stratton M.R.;
RT   "Patterns of somatic mutation in human cancer genomes.";
RL   Nature 446:153-158(2007).
CC   -!- FUNCTION: Binds to the IL-1 type I receptor following IL-1 engagement,
CC       triggering intracellular signaling cascades leading to transcriptional
CC       up-regulation and mRNA stabilization. {ECO:0000269|PubMed:10383454,
CC       ECO:0000269|PubMed:9374458}.
CC   -!- SUBUNIT: Interacts with MYD88. IL-1 stimulation leads to the formation
CC       of a signaling complex which dissociates from the IL-1 receptor
CC       following the binding of PELI1. {ECO:0000269|PubMed:9374458}.
CC   -!- INTERACTION:
CC       O43187; P10398: ARAF; NbExp=2; IntAct=EBI-447733, EBI-365961;
CC       O43187; Q9NWZ3: IRAK4; NbExp=6; IntAct=EBI-447733, EBI-448378;
CC       O43187; P46977: STT3A; NbExp=2; IntAct=EBI-447733, EBI-719212;
CC       O43187; Q13148: TARDBP; NbExp=2; IntAct=EBI-447733, EBI-372899;
CC       O43187; P58753: TIRAP; NbExp=2; IntAct=EBI-447733, EBI-528644;
CC       O43187; Q9H0E2: TOLLIP; NbExp=2; IntAct=EBI-447733, EBI-74615;
CC       O43187; Q9Y4K3: TRAF6; NbExp=3; IntAct=EBI-447733, EBI-359276;
CC       O43187; Q5D1E8: ZC3H12A; NbExp=2; IntAct=EBI-447733, EBI-747793;
CC       O43187; P68467: OPG044; Xeno; NbExp=2; IntAct=EBI-447733, EBI-8022707;
CC       O43187; Q6PDS3: Sarm1; Xeno; NbExp=2; IntAct=EBI-447733, EBI-6117196;
CC   -!- TISSUE SPECIFICITY: Expressed in spleen, thymus, prostate, lung, liver,
CC       skeletal muscle, kidney, pancreas and peripheral blood leukocytes.
CC       {ECO:0000269|PubMed:9374458}.
CC   -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC       inactive.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC       protein kinase family. Pelle subfamily. {ECO:0000305}.
CC   -!- CAUTION: Asn-335 is present instead of the conserved Asp which is
CC       expected to be an active site residue. This enzyme has been shown to be
CC       catalytically inactive. {ECO:0000305}.
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DR   EMBL; AJ496794; CAD43180.3; -; mRNA.
DR   EMBL; AK299033; BAG61108.1; -; mRNA.
DR   EMBL; BC125184; AAI25185.1; -; mRNA.
DR   EMBL; AF026273; AAB87669.1; -; mRNA.
DR   CCDS; CCDS33697.1; -.
DR   RefSeq; NP_001561.3; NM_001570.3.
DR   PDB; 3MOP; X-ray; 3.40 A; K/L/M/N=2-112.
DR   PDBsum; 3MOP; -.
DR   AlphaFoldDB; O43187; -.
DR   SMR; O43187; -.
DR   BioGRID; 109865; 64.
DR   CORUM; O43187; -.
DR   DIP; DIP-31800N; -.
DR   ELM; O43187; -.
DR   IntAct; O43187; 47.
DR   MINT; O43187; -.
DR   STRING; 9606.ENSP00000256458; -.
DR   BindingDB; O43187; -.
DR   ChEMBL; CHEMBL4105759; -.
DR   GlyGen; O43187; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; O43187; -.
DR   PhosphoSitePlus; O43187; -.
DR   BioMuta; IRAK2; -.
DR   CPTAC; CPTAC-1319; -.
DR   EPD; O43187; -.
DR   jPOST; O43187; -.
DR   MassIVE; O43187; -.
DR   MaxQB; O43187; -.
DR   PaxDb; 9606-ENSP00000256458; -.
DR   PeptideAtlas; O43187; -.
DR   ProteomicsDB; 48804; -.
DR   Antibodypedia; 4605; 777 antibodies from 42 providers.
DR   DNASU; 3656; -.
DR   Ensembl; ENST00000256458.5; ENSP00000256458.4; ENSG00000134070.5.
DR   GeneID; 3656; -.
DR   KEGG; hsa:3656; -.
DR   MANE-Select; ENST00000256458.5; ENSP00000256458.4; NM_001570.4; NP_001561.3.
DR   UCSC; uc003bve.2; human.
DR   AGR; HGNC:6113; -.
DR   CTD; 3656; -.
DR   DisGeNET; 3656; -.
DR   GeneCards; IRAK2; -.
DR   HGNC; HGNC:6113; IRAK2.
DR   HPA; ENSG00000134070; Tissue enhanced (bone).
DR   MIM; 603304; gene.
DR   neXtProt; NX_O43187; -.
DR   OpenTargets; ENSG00000134070; -.
DR   PharmGKB; PA29913; -.
DR   VEuPathDB; HostDB:ENSG00000134070; -.
DR   eggNOG; KOG1187; Eukaryota.
DR   GeneTree; ENSGT00940000159835; -.
DR   HOGENOM; CLU_000288_173_0_1; -.
DR   InParanoid; O43187; -.
DR   OMA; ALSEWDW; -.
DR   OrthoDB; 2999496at2759; -.
DR   PhylomeDB; O43187; -.
DR   TreeFam; TF328924; -.
DR   BRENDA; 2.7.10.2; 2681.
DR   PathwayCommons; O43187; -.
DR   Reactome; R-HSA-166058; MyD88:MAL(TIRAP) cascade initiated on plasma membrane.
DR   Reactome; R-HSA-168638; NOD1/2 Signaling Pathway.
DR   Reactome; R-HSA-445989; TAK1-dependent IKK and NF-kappa-B activation.
DR   Reactome; R-HSA-450302; activated TAK1 mediates p38 MAPK activation.
DR   Reactome; R-HSA-450321; JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
DR   Reactome; R-HSA-9020702; Interleukin-1 signaling.
DR   Reactome; R-HSA-937042; IRAK2 mediated activation of TAK1 complex.
DR   Reactome; R-HSA-937072; TRAF6-mediated induction of TAK1 complex within TLR4 complex.
DR   Reactome; R-HSA-9692916; SARS-CoV-1 activates/modulates innate immune responses.
DR   Reactome; R-HSA-9705671; SARS-CoV-2 activates/modulates innate and adaptive immune responses.
DR   Reactome; R-HSA-975138; TRAF6 mediated induction of NFkB and MAP kinases upon TLR7/8 or 9 activation.
DR   Reactome; R-HSA-975155; MyD88 dependent cascade initiated on endosome.
DR   Reactome; R-HSA-975163; IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation.
DR   Reactome; R-HSA-975871; MyD88 cascade initiated on plasma membrane.
DR   SignaLink; O43187; -.
DR   SIGNOR; O43187; -.
DR   BioGRID-ORCS; 3656; 7 hits in 1185 CRISPR screens.
DR   ChiTaRS; IRAK2; human.
DR   EvolutionaryTrace; O43187; -.
DR   GeneWiki; IRAK2; -.
DR   GenomeRNAi; 3656; -.
DR   Pharos; O43187; Tbio.
DR   PRO; PR:O43187; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; O43187; Protein.
DR   Bgee; ENSG00000134070; Expressed in cartilage tissue and 149 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0010008; C:endosome membrane; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0060090; F:molecular adaptor activity; IDA:UniProt.
DR   GO; GO:0046982; F:protein heterodimerization activity; IPI:BHF-UCL.
DR   GO; GO:0042803; F:protein homodimerization activity; IPI:BHF-UCL.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0035591; F:signaling adaptor activity; IDA:UniProt.
DR   GO; GO:0007249; P:canonical NF-kappaB signal transduction; IDA:UniProt.
DR   GO; GO:0071222; P:cellular response to lipopolysaccharide; IBA:GO_Central.
DR   GO; GO:0006954; P:inflammatory response; TAS:ProtInc.
DR   GO; GO:0070498; P:interleukin-1-mediated signaling pathway; IMP:BHF-UCL.
DR   GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR   GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IEA:Ensembl.
DR   GO; GO:0002755; P:MyD88-dependent toll-like receptor signaling pathway; TAS:BHF-UCL.
DR   GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IMP:BHF-UCL.
DR   GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:BHF-UCL.
DR   GO; GO:0006468; P:protein phosphorylation; TAS:ProtInc.
DR   GO; GO:0001959; P:regulation of cytokine-mediated signaling pathway; IMP:BHF-UCL.
DR   GO; GO:0070555; P:response to interleukin-1; IMP:BHF-UCL.
DR   GO; GO:0008063; P:Toll signaling pathway; IBA:GO_Central.
DR   GO; GO:0034142; P:toll-like receptor 4 signaling pathway; IDA:UniProt.
DR   CDD; cd08795; Death_IRAK2; 1.
DR   CDD; cd14157; STKc_IRAK2; 1.
DR   Gene3D; 1.10.533.10; Death Domain, Fas; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011029; DEATH-like_dom_sf.
DR   InterPro; IPR000488; Death_domain.
DR   InterPro; IPR042151; Death_IRAK2.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   PANTHER; PTHR24419; INTERLEUKIN-1 RECEPTOR-ASSOCIATED KINASE; 1.
DR   PANTHER; PTHR24419:SF2; INTERLEUKIN-1 RECEPTOR-ASSOCIATED KINASE-LIKE 2; 1.
DR   Pfam; PF00531; Death; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SUPFAM; SSF47986; DEATH domain; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   Genevisible; O43187; HS.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..625
FT                   /note="Interleukin-1 receptor-associated kinase-like 2"
FT                   /id="PRO_0000086032"
FT   DOMAIN          13..94
FT                   /note="Death"
FT   DOMAIN          210..489
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          111..181
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          510..540
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        115..131
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        166..181
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        514..540
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         216..224
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         237
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         337..340
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         144
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VARIANT         43
FT                   /note="R -> Q (in dbSNP:rs34945585)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_041342"
FT   VARIANT         47
FT                   /note="S -> Y (in dbSNP:rs11465864)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_030527"
FT   VARIANT         99
FT                   /note="I -> V (in dbSNP:rs55898544)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_041343"
FT   VARIANT         147
FT                   /note="R -> T (in dbSNP:rs56053222)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_041344"
FT   VARIANT         214
FT                   /note="R -> G (in dbSNP:rs35060588)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_041345"
FT   VARIANT         249
FT                   /note="S -> L (in a lung adenocarcinoma sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_041346"
FT   VARIANT         392
FT                   /note="L -> V (in dbSNP:rs3844283)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_030528"
FT   VARIANT         421
FT                   /note="P -> T (in a lung adenocarcinoma sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_041347"
FT   VARIANT         431
FT                   /note="D -> E (in dbSNP:rs708035)"
FT                   /evidence="ECO:0000269|PubMed:17344846,
FT                   ECO:0000269|PubMed:9374458, ECO:0000269|Ref.1"
FT                   /id="VAR_030529"
FT   VARIANT         439
FT                   /note="L -> V (in dbSNP:rs11465927)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_030530"
FT   VARIANT         469
FT                   /note="D -> N (in dbSNP:rs56242986)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_041348"
FT   VARIANT         503
FT                   /note="L -> I (in dbSNP:rs9854688)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_030531"
FT   VARIANT         566
FT                   /note="R -> W (in dbSNP:rs55740652)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_041349"
FT   VARIANT         574
FT                   /note="D -> H (in dbSNP:rs11465930)"
FT                   /id="VAR_030532"
FT   HELIX           5..7
FT                   /evidence="ECO:0007829|PDB:3MOP"
FT   HELIX           10..16
FT                   /evidence="ECO:0007829|PDB:3MOP"
FT   TURN            17..22
FT                   /evidence="ECO:0007829|PDB:3MOP"
FT   HELIX           25..32
FT                   /evidence="ECO:0007829|PDB:3MOP"
FT   TURN            33..36
FT                   /evidence="ECO:0007829|PDB:3MOP"
FT   HELIX           39..47
FT                   /evidence="ECO:0007829|PDB:3MOP"
FT   HELIX           48..50
FT                   /evidence="ECO:0007829|PDB:3MOP"
FT   HELIX           56..65
FT                   /evidence="ECO:0007829|PDB:3MOP"
FT   TURN            66..68
FT                   /evidence="ECO:0007829|PDB:3MOP"
FT   HELIX           72..76
FT                   /evidence="ECO:0007829|PDB:3MOP"
FT   TURN            77..81
FT                   /evidence="ECO:0007829|PDB:3MOP"
FT   HELIX           84..87
FT                   /evidence="ECO:0007829|PDB:3MOP"
FT   TURN            88..91
FT                   /evidence="ECO:0007829|PDB:3MOP"
SQ   SEQUENCE   625 AA;  69433 MW;  715C954BC9452710 CRC64;
     MACYIYQLPS WVLDDLCRNM DALSEWDWME FASYVITDLT QLRKIKSMER VQGVSITREL
     LWWWGMRQAT VQQLVDLLCR LELYRAAQII LNWKPAPEIR CPIPAFPDSV KPEKPLAASV
     RKAEDEQEEG QPVRMATFPG PGSSPARAHQ PAFLQPPEED APHSLRSDLP TSSDSKDFST
     SIPKQEKLLS LAGDSLFWSE ADVVQATDDF NQNRKISQGT FADVYRGHRH GKPFVFKKLR
     ETACSSPGSI ERFFQAELQI CLRCCHPNVL PVLGFCAARQ FHSFIYPYMA NGSLQDRLQG
     QGGSDPLPWP QRVSICSGLL CAVEYLHGLE IIHSNVKSSN VLLDQNLTPK LAHPMAHLCP
     VNKRSKYTMM KTHLLRTSAA YLPEDFIRVG QLTKRVDIFS CGIVLAEVLT GIPAMDNNRS
     PVYLKDLLLS DIPSSTASLC SRKTGVENVM AKEICQKYLE KGAGRLPEDC AEALATAACL
     CLRRRNTSLQ EVCGSVAAVE ERLRGRETLL PWSGLSEGTG SSSNTPEETD DVDNSSLDAS
     SSMSVAPWAG AATPLLPTEN GEGRLRVIVG READSSSEAC VGLEPPQDVT ETSWQIEINE
     AKRKLMENIL LYKEEKVDSI ELFGP
//