BIRC3_HUMAN
ID BIRC3_HUMAN Reviewed; 604 AA.
AC Q13489; Q16628; Q9HC27; Q9UP46;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 215.
DE RecName: Full=Baculoviral IAP repeat-containing protein 3;
DE EC=2.3.2.27 {ECO:0000269|PubMed:21931591, ECO:0000269|PubMed:23453969};
DE AltName: Full=Apoptosis inhibitor 2;
DE Short=API2;
DE AltName: Full=Cellular inhibitor of apoptosis 2;
DE Short=C-IAP2 {ECO:0000303|PubMed:8548810};
DE AltName: Full=IAP homolog C;
DE AltName: Full=Inhibitor of apoptosis protein 1;
DE Short=hIAP-1;
DE Short=hIAP1;
DE AltName: Full=RING finger protein 49;
DE AltName: Full=RING-type E3 ubiquitin transferase BIRC3 {ECO:0000305};
DE AltName: Full=TNFR2-TRAF-signaling complex protein 1;
GN Name=BIRC3; Synonyms=API2, MIHC, RNF49;
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].
RX PubMed=8548810; DOI=10.1016/0092-8674(95)90149-3;
RA Rothe M., Pan M.-G., Henzel W.J., Ayres T.M., Goeddel D.V.;
RT "The TNFR2-TRAF signaling complex contains two novel proteins related to
RT baculoviral inhibitor of apoptosis proteins.";
RL Cell 83:1243-1252(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=8552191; DOI=10.1038/379349a0;
RA Liston P., Roy N., Tamai K., Lefebvre C., Baird S., Cherton-Horvat G.,
RA Farahani R., McLean M., Ikeda J., Mackenzie A., Korneluk R.G.;
RT "Suppression of apoptosis in mammalian cells by NAIP and a related family
RT of IAP genes.";
RL Nature 379:349-353(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fetal liver;
RX PubMed=8643514; DOI=10.1073/pnas.93.10.4974;
RA Uren A.G., Pakusch M., Hawkins C.J., Puls K.L., Vaux D.L.;
RT "Cloning and expression of apoptosis inhibitory protein homologs that
RT function to inhibit apoptosis and/or bind tumor necrosis factor receptor-
RT associated factors.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:4974-4978(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10233894;
RA Horrevoets A.J.G., Fontijn R.D., van Zonneveld A.J., de Vries C.J.M.,
RA ten Cate J.W., Pannekoek H.;
RT "Vascular endothelial genes that are responsive to tumor necrosis factor-
RT alpha in vitro are expressed in atherosclerotic lesions, including
RT inhibitor of apoptosis protein-1, stannin, and two novel genes.";
RL Blood 93:3418-3431(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARG-260 AND LYS-401.
RG NIEHS SNPs program;
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lymph;
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 [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 362-441.
RX PubMed=11066071;
RX DOI=10.1002/1098-2264(2000)9999:9999<::aid-gcc1036>3.0.co;2-i;
RA Baens M., Steyls A., Dierlamm J., De Wolf-Peeters C., Marynen P.;
RT "Structure of the MLT gene and molecular characterization of the genomic
RT breakpoint junctions in the t(11;18)(q21;q21) of marginal zone B-cell
RT lymphomas of MALT type.";
RL Genes Chromosomes Cancer 29:281-291(2000).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=15665297;
RA Samuel T., Okada K., Hyer M., Welsh K., Zapata J.M., Reed J.C.;
RT "cIAP1 Localizes to the nuclear compartment and modulates the cell cycle.";
RL Cancer Res. 65:210-218(2005).
RN [9]
RP REVIEW ON FUNCTION.
RX PubMed=18414036; DOI=10.4161/cc.7.8.5783;
RA Dubrez-Daloz L., Dupoux A., Cartier J.;
RT "IAPs: more than just inhibitors of apoptosis proteins.";
RL Cell Cycle 7:1036-1046(2008).
RN [10]
RP REVIEW ON FUNCTION.
RX PubMed=20888210; DOI=10.1016/j.ceb.2010.08.025;
RA Lopez J., Meier P.;
RT "To fight or die - inhibitor of apoptosis proteins at the crossroad of
RT innate immunity and death.";
RL Curr. Opin. Cell Biol. 22:872-881(2010).
RN [11]
RP REVIEW ON FUNCTION.
RX PubMed=20651737; DOI=10.1038/nrc2889;
RA Gyrd-Hansen M., Meier P.;
RT "IAPs: from caspase inhibitors to modulators of NF-kappaB, inflammation and
RT cancer.";
RL Nat. Rev. Cancer 10:561-574(2010).
RN [12]
RP REVIEW ON FUNCTION.
RX PubMed=21447281;
RA Damgaard R.B., Gyrd-Hansen M.;
RT "Inhibitor of apoptosis (IAP) proteins in regulation of inflammation and
RT innate immunity.";
RL Discov. Med. 11:221-231(2011).
RN [13]
RP ACTIVITY REGULATION, AND INTERACTION WITH USP19.
RX PubMed=21849505; DOI=10.1074/jbc.m111.282020;
RA Mei Y., Hahn A.A., Hu S., Yang X.;
RT "The USP19 deubiquitinase regulates the stability of c-IAP1 and c-IAP2.";
RL J. Biol. Chem. 286:35380-35387(2011).
RN [14]
RP FUNCTION IN THE UBIQUITINATION OF RIPK1; RIPK2; RIPK3 AND RIPK4,
RP INTERACTION WITH RIPK1; RIPK2; RIPK3 AND RIPK4, AND CATALYTIC ACTIVITY.
RX PubMed=21931591; DOI=10.1371/journal.pone.0022356;
RA Bertrand M.J., Lippens S., Staes A., Gilbert B., Roelandt R., De Medts J.,
RA Gevaert K., Declercq W., Vandenabeele P.;
RT "cIAP1/2 are direct E3 ligases conjugating diverse types of ubiquitin
RT chains to receptor interacting proteins kinases 1 to 4 (RIP1-4).";
RL PLoS ONE 6:E22356-E22356(2011).
RN [15]
RP REVIEW ON FUNCTION.
RX PubMed=22095281; DOI=10.1038/cdd.2011.163;
RA Darding M., Meier P.;
RT "IAPs: guardians of RIPK1.";
RL Cell Death Differ. 19:58-66(2012).
RN [16]
RP FUNCTION IN IKBKE UBIQUITINATION, AND CATALYTIC ACTIVITY.
RX PubMed=23453969; DOI=10.1016/j.celrep.2013.01.031;
RA Zhou A.Y., Shen R.R., Kim E., Lock Y.J., Xu M., Chen Z.J., Hahn W.C.;
RT "IKKepsilon-mediated tumorigenesis requires K63-linked polyubiquitination
RT by a cIAP1/cIAP2/TRAF2 E3 ubiquitin ligase complex.";
RL Cell Rep. 3:724-733(2013).
CC -!- FUNCTION: Multi-functional protein which regulates not only caspases
CC and apoptosis, but also modulates inflammatory signaling and immunity,
CC mitogenic kinase signaling and cell proliferation, as well as cell
CC invasion and metastasis. Acts as an E3 ubiquitin-protein ligase
CC regulating NF-kappa-B signaling and regulates both canonical and non-
CC canonical NF-kappa-B signaling by acting in opposite directions: acts
CC as a positive regulator of the canonical pathway and suppresses
CC constitutive activation of non-canonical NF-kappa-B signaling. The
CC target proteins for its E3 ubiquitin-protein ligase activity include:
CC RIPK1, RIPK2, RIPK3, RIPK4, CASP3, CASP7, CASP8, IKBKE, TRAF1, and
CC BCL10. Acts as an important regulator of innate immune signaling via
CC regulation of Toll-like receptors (TLRs), Nodlike receptors (NLRs) and
CC RIG-I like receptors (RLRs), collectively referred to as pattern
CC recognition receptors (PRRs). Protects cells from spontaneous formation
CC of the ripoptosome, a large multi-protein complex that has the
CC capability to kill cancer cells in a caspase-dependent and caspase-
CC independent manner. Suppresses ripoptosome formation by ubiquitinating
CC RIPK1 and CASP8. {ECO:0000269|PubMed:21931591,
CC ECO:0000269|PubMed:23453969}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000269|PubMed:21931591,
CC ECO:0000269|PubMed:23453969};
CC -!- ACTIVITY REGULATION: USP19 regulates the stability of BIRC3/c-IAP2 by
CC preventing its ubiquitination. {ECO:0000269|PubMed:21849505}.
CC -!- SUBUNIT: Interacts with PRSS25; interaction inhibits apoptotic
CC suppressor activity. The BIR motifs region interacts with TNF receptor
CC associated factors 1 and 2 (TRAF1 and TRAF2) to form a heteromeric
CC complex, which is then recruited to the tumor necrosis factor receptor
CC 2 (TNFR2). Interaction with TRAF2 is required for ubiquitination of
CC IKBKE, degradation of NFKBIA and activation of NF-kappa-B. Interacts
CC with RIP1, RIP2, RIP3, RIP4 and USP19. {ECO:0000269|PubMed:21849505,
CC ECO:0000269|PubMed:21931591}.
CC -!- INTERACTION:
CC Q13489; Q13546: RIPK1; NbExp=3; IntAct=EBI-517709, EBI-358507;
CC Q13489; O43353: RIPK2; NbExp=3; IntAct=EBI-517709, EBI-358522;
CC Q13489; Q9Y572: RIPK3; NbExp=3; IntAct=EBI-517709, EBI-298250;
CC Q13489; P57078: RIPK4; NbExp=3; IntAct=EBI-517709, EBI-4422308;
CC Q13489; Q12933: TRAF2; NbExp=7; IntAct=EBI-517709, EBI-355744;
CC Q13489; P62837: UBE2D2; NbExp=2; IntAct=EBI-517709, EBI-347677;
CC Q13489; P61088: UBE2N; NbExp=2; IntAct=EBI-517709, EBI-1052908;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15665297}. Nucleus
CC {ECO:0000269|PubMed:15665297}.
CC -!- TISSUE SPECIFICITY: Highly expressed in fetal lung, and kidney. In the
CC adult, expression is mainly seen in lymphoid tissues, including spleen,
CC thymus and peripheral blood lymphocytes.
CC -!- PTM: Auto-ubiquitinated and degraded by the proteasome in apoptotic
CC cells.
CC -!- DISEASE: Note=A chromosomal aberration involving BIRC3 is recurrent in
CC low-grade mucosa-associated lymphoid tissue (MALT lymphoma).
CC Translocation t(11;18)(q21;q21) with MALT1. This translocation is found
CC in approximately 50% of cytogenetically abnormal low-grade MALT
CC lymphoma.
CC -!- SIMILARITY: Belongs to the IAP family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/BIRC3ID239.html";
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/birc3/";
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; L49432; AAC41943.1; -; mRNA.
DR EMBL; U45878; AAC50371.1; -; mRNA.
DR EMBL; U37546; AAC50507.1; -; mRNA.
DR EMBL; AF070674; AAC83232.1; -; mRNA.
DR EMBL; AY764389; AAU88144.1; -; Genomic_DNA.
DR EMBL; BC037420; AAH37420.1; -; mRNA.
DR EMBL; AF178945; AAG09369.1; -; Genomic_DNA.
DR CCDS; CCDS8315.1; -.
DR PIR; S68449; S68449.
DR RefSeq; NP_001156.1; NM_001165.4.
DR RefSeq; NP_892007.1; NM_182962.2.
DR RefSeq; XP_016873132.1; XM_017017643.1.
DR PDB; 2UVL; X-ray; 1.91 A; A/B=244-337.
DR PDB; 3EB5; X-ray; 2.00 A; A=536-604.
DR PDB; 3EB6; X-ray; 3.40 A; A=536-604.
DR PDB; 3M0A; X-ray; 2.61 A; D=26-99.
DR PDB; 3M0D; X-ray; 2.80 A; D=26-99.
DR PDB; 7NK0; X-ray; 3.30 A; D/E=26-102.
DR PDBsum; 2UVL; -.
DR PDBsum; 3EB5; -.
DR PDBsum; 3EB6; -.
DR PDBsum; 3M0A; -.
DR PDBsum; 3M0D; -.
DR PDBsum; 7NK0; -.
DR AlphaFoldDB; Q13489; -.
DR SMR; Q13489; -.
DR BioGRID; 106827; 1320.
DR CORUM; Q13489; -.
DR DIP; DIP-33720N; -.
DR IntAct; Q13489; 41.
DR MINT; Q13489; -.
DR STRING; 9606.ENSP00000263464; -.
DR BindingDB; Q13489; -.
DR ChEMBL; CHEMBL5335; -.
DR GuidetoPHARMACOLOGY; 2792; -.
DR MEROPS; I32.003; -.
DR MEROPS; I32.007; -.
DR iPTMnet; Q13489; -.
DR PhosphoSitePlus; Q13489; -.
DR BioMuta; BIRC3; -.
DR DMDM; 2497236; -.
DR EPD; Q13489; -.
DR jPOST; Q13489; -.
DR MassIVE; Q13489; -.
DR MaxQB; Q13489; -.
DR PaxDb; Q13489; -.
DR PeptideAtlas; Q13489; -.
DR PRIDE; Q13489; -.
DR ProteomicsDB; 59483; -.
DR Antibodypedia; 1035; 709 antibodies from 41 providers.
DR DNASU; 330; -.
DR Ensembl; ENST00000263464.9; ENSP00000263464.4; ENSG00000023445.16.
DR Ensembl; ENST00000526421.6; ENSP00000501119.1; ENSG00000023445.16.
DR Ensembl; ENST00000532808.5; ENSP00000432907.1; ENSG00000023445.16.
DR Ensembl; ENST00000615299.4; ENSP00000481903.1; ENSG00000023445.16.
DR GeneID; 330; -.
DR KEGG; hsa:330; -.
DR MANE-Select; ENST00000263464.9; ENSP00000263464.4; NM_001165.5; NP_001156.1.
DR UCSC; uc001pgx.5; human.
DR CTD; 330; -.
DR DisGeNET; 330; -.
DR GeneCards; BIRC3; -.
DR HGNC; HGNC:591; BIRC3.
DR HPA; ENSG00000023445; Tissue enhanced (intestine, lymphoid tissue).
DR MalaCards; BIRC3; -.
DR MIM; 601721; gene.
DR neXtProt; NX_Q13489; -.
DR OpenTargets; ENSG00000023445; -.
DR Orphanet; 52417; MALT lymphoma.
DR PharmGKB; PA25360; -.
DR VEuPathDB; HostDB:ENSG00000023445; -.
DR eggNOG; KOG1101; Eukaryota.
DR GeneTree; ENSGT00940000154175; -.
DR HOGENOM; CLU_016347_1_1_1; -.
DR InParanoid; Q13489; -.
DR OrthoDB; 1340284at2759; -.
DR PhylomeDB; Q13489; -.
DR TreeFam; TF105356; -.
DR BRENDA; 2.3.2.27; 2681.
DR PathwayCommons; Q13489; -.
DR Reactome; R-HSA-168638; NOD1/2 Signaling Pathway.
DR Reactome; R-HSA-168927; TICAM1, RIP1-mediated IKK complex recruitment.
DR Reactome; R-HSA-5213460; RIPK1-mediated regulated necrosis.
DR Reactome; R-HSA-5357905; Regulation of TNFR1 signaling.
DR Reactome; R-HSA-5357956; TNFR1-induced NFkappaB signaling pathway.
DR Reactome; R-HSA-5668541; TNFR2 non-canonical NF-kB pathway.
DR Reactome; R-HSA-5675482; Regulation of necroptotic cell death.
DR Reactome; R-HSA-5676594; TNF receptor superfamily (TNFSF) members mediating non-canonical NF-kB pathway.
DR Reactome; R-HSA-5689880; Ub-specific processing proteases.
DR Reactome; R-HSA-937041; IKK complex recruitment mediated by RIP1.
DR SignaLink; Q13489; -.
DR SIGNOR; Q13489; -.
DR BioGRID-ORCS; 330; 17 hits in 1112 CRISPR screens.
DR ChiTaRS; BIRC3; human.
DR EvolutionaryTrace; Q13489; -.
DR GeneWiki; Baculoviral_IAP_repeat-containing_protein_3; -.
DR GenomeRNAi; 330; -.
DR Pharos; Q13489; Tchem.
DR PRO; PR:Q13489; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q13489; protein.
DR Bgee; ENSG00000023445; Expressed in vermiform appendix and 153 other tissues.
DR ExpressionAtlas; Q13489; baseline and differential.
DR Genevisible; Q13489; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0045121; C:membrane raft; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0016740; F:transferase activity; EXP:Reactome.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; TAS:Reactome.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IBA:GO_Central.
DR GO; GO:0060546; P:negative regulation of necroptotic process; IBA:GO_Central.
DR GO; GO:0038061; P:NIK/NF-kappaB signaling; TAS:UniProtKB.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; TAS:UniProtKB.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; IDA:UniProtKB.
DR GO; GO:0042981; P:regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; IBA:GO_Central.
DR GO; GO:2000116; P:regulation of cysteine-type endopeptidase activity; TAS:UniProtKB.
DR GO; GO:0050727; P:regulation of inflammatory response; TAS:UniProtKB.
DR GO; GO:0045088; P:regulation of innate immune response; TAS:UniProtKB.
DR GO; GO:0060544; P:regulation of necroptotic process; IMP:UniProtKB.
DR GO; GO:0070424; P:regulation of nucleotide-binding oligomerization domain containing signaling pathway; TAS:UniProtKB.
DR GO; GO:0039535; P:regulation of RIG-I signaling pathway; TAS:UniProtKB.
DR GO; GO:0034121; P:regulation of toll-like receptor signaling pathway; TAS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; TAS:Reactome.
DR CDD; cd00022; BIR; 3.
DR Gene3D; 1.10.533.10; -; 1.
DR InterPro; IPR001370; BIR_rpt.
DR InterPro; IPR001315; CARD.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR001841; Znf_RING.
DR Pfam; PF00653; BIR; 3.
DR Pfam; PF00619; CARD; 1.
DR SMART; SM00238; BIR; 3.
DR SMART; SM00114; CARD; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF47986; SSF47986; 1.
DR PROSITE; PS01282; BIR_REPEAT_1; 3.
DR PROSITE; PS50143; BIR_REPEAT_2; 3.
DR PROSITE; PS50209; CARD; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Apoptosis; Chromosomal rearrangement; Cytoplasm;
KW Metal-binding; Nucleus; Reference proteome; Repeat; Transferase;
KW Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..604
FT /note="Baculoviral IAP repeat-containing protein 3"
FT /id="PRO_0000122349"
FT REPEAT 29..96
FT /note="BIR 1"
FT REPEAT 169..235
FT /note="BIR 2"
FT REPEAT 255..322
FT /note="BIR 3"
FT DOMAIN 439..529
FT /note="CARD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00046"
FT ZN_FING 557..592
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT BINDING 292
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00029"
FT BINDING 295
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00029"
FT BINDING 312
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00029"
FT BINDING 319
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00029"
FT SITE 442..443
FT /note="Breakpoint for translocation to form BIRC3-MALT1"
FT VARIANT 260
FT /note="K -> R (in dbSNP:rs2276113)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_021069"
FT VARIANT 386
FT /note="V -> M (in dbSNP:rs12222256)"
FT /id="VAR_049536"
FT VARIANT 401
FT /note="R -> K (in dbSNP:rs17881197)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_021070"
FT CONFLICT 18
FT /note="N -> Y (in Ref. 4; AAC83232)"
FT /evidence="ECO:0000305"
FT CONFLICT 119
FT /note="N -> H (in Ref. 2; AAC50371)"
FT /evidence="ECO:0000305"
FT CONFLICT 153
FT /note="D -> E (in Ref. 2; AAC50371)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="H -> P (in Ref. 2; AAC50371)"
FT /evidence="ECO:0000305"
FT CONFLICT 165
FT /note="A -> P (in Ref. 2; AAC50371)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="K -> R (in Ref. 2; AAC50371)"
FT /evidence="ECO:0000305"
FT CONFLICT 364
FT /note="F -> L (in Ref. 2; AAC50371)"
FT /evidence="ECO:0000305"
FT CONFLICT 552
FT /note="Q -> P (in Ref. 2; AAC50371)"
FT /evidence="ECO:0000305"
FT HELIX 28..34
FT /evidence="ECO:0007829|PDB:3M0A"
FT HELIX 35..38
FT /evidence="ECO:0007829|PDB:3M0A"
FT HELIX 47..52
FT /evidence="ECO:0007829|PDB:3M0A"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:3M0A"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:3M0A"
FT TURN 67..69
FT /evidence="ECO:0007829|PDB:3M0A"
FT HELIX 82..89
FT /evidence="ECO:0007829|PDB:3M0A"
FT TURN 94..97
FT /evidence="ECO:0007829|PDB:3M0A"
FT HELIX 250..252
FT /evidence="ECO:0007829|PDB:2UVL"
FT HELIX 255..260
FT /evidence="ECO:0007829|PDB:2UVL"
FT HELIX 261..264
FT /evidence="ECO:0007829|PDB:2UVL"
FT HELIX 273..278
FT /evidence="ECO:0007829|PDB:2UVL"
FT STRAND 281..285
FT /evidence="ECO:0007829|PDB:2UVL"
FT TURN 286..288
FT /evidence="ECO:0007829|PDB:2UVL"
FT STRAND 289..292
FT /evidence="ECO:0007829|PDB:2UVL"
FT TURN 293..295
FT /evidence="ECO:0007829|PDB:2UVL"
FT STRAND 298..301
FT /evidence="ECO:0007829|PDB:2UVL"
FT HELIX 308..315
FT /evidence="ECO:0007829|PDB:2UVL"
FT HELIX 320..334
FT /evidence="ECO:0007829|PDB:2UVL"
FT HELIX 544..555
FT /evidence="ECO:0007829|PDB:3EB5"
FT TURN 558..560
FT /evidence="ECO:0007829|PDB:3EB5"
FT STRAND 561..564
FT /evidence="ECO:0007829|PDB:3EB5"
FT STRAND 567..570
FT /evidence="ECO:0007829|PDB:3EB5"
FT STRAND 575..577
FT /evidence="ECO:0007829|PDB:3EB5"
FT TURN 579..581
FT /evidence="ECO:0007829|PDB:3EB5"
FT HELIX 582..584
FT /evidence="ECO:0007829|PDB:3EB5"
FT STRAND 589..591
FT /evidence="ECO:0007829|PDB:3EB5"
FT STRAND 597..600
FT /evidence="ECO:0007829|PDB:3EB5"
SQ SEQUENCE 604 AA; 68372 MW; 8581A00BA9AAB4A7 CRC64;
MNIVENSIFL SNLMKSANTF ELKYDLSCEL YRMSTYSTFP AGVPVSERSL ARAGFYYTGV
NDKVKCFCCG LMLDNWKRGD SPTEKHKKLY PSCRFVQSLN SVNNLEATSQ PTFPSSVTNS
THSLLPGTEN SGYFRGSYSN SPSNPVNSRA NQDFSALMRS SYHCAMNNEN ARLLTFQTWP
LTFLSPTDLA KAGFYYIGPG DRVACFACGG KLSNWEPKDN AMSEHLRHFP KCPFIENQLQ
DTSRYTVSNL SMQTHAARFK TFFNWPSSVL VNPEQLASAG FYYVGNSDDV KCFCCDGGLR
CWESGDDPWV QHAKWFPRCE YLIRIKGQEF IRQVQASYPH LLEQLLSTSD SPGDENAESS
IIHFEPGEDH SEDAIMMNTP VINAAVEMGF SRSLVKQTVQ RKILATGENY RLVNDLVLDL
LNAEDEIREE ERERATEEKE SNDLLLIRKN RMALFQHLTC VIPILDSLLT AGIINEQEHD
VIKQKTQTSL QARELIDTIL VKGNIAATVF RNSLQEAEAV LYEHLFVQQD IKYIPTEDVS
DLPVEEQLRR LQEERTCKVC MDKEVSIVFI PCGHLVVCKD CAPSLRKCPI CRSTIKGTVR
TFLS
