ID NALP7_HUMAN Reviewed; 980 AA. AC Q8WX94; E9PE16; Q32MH8; Q7RTR1; DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 1. DT 27-MAR-2024, entry version 182. DE RecName: Full=NACHT, LRR and PYD domains-containing protein 7; DE AltName: Full=Nucleotide-binding oligomerization domain protein 12; DE AltName: Full=PYRIN-containing APAF1-like protein 3; GN Name=NLRP7; Synonyms=NALP7, NOD12, PYPAF3; 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). RX PubMed=12019269; DOI=10.1074/jbc.m203915200; RA Wang L., Manji G.A., Grenier J.M., Al-Garawi A., Merriam S., Lora J.M., RA Geddes B.J., Briskin M., DiStefano P.S., Bertin J.; RT "PYPAF7, a novel PYRIN-containing Apaf1-like protein that regulates RT activation of NF-kappa B and caspase-1-dependent cytokine processing."; RL J. Biol. Chem. 277:29874-29880(2002). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=12563287; DOI=10.1038/nrm1019; RA Tschopp J., Martinon F., Burns K.; RT "NALPs: a novel protein family involved in inflammation."; RL Nat. Rev. Mol. Cell Biol. 4:95-104(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057824; DOI=10.1038/nature02399; RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A., RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., RA Rubin E.M., Lucas S.M.; RT "The DNA sequence and biology of human chromosome 19."; RL Nature 428:529-535(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). 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 IDENTIFICATION (ISOFORM 2). RX PubMed=12766759; DOI=10.1038/nri1086; RA Inohara N., Nunez G.; RT "NODs: intracellular proteins involved in inflammation and apoptosis."; RL Nat. Rev. Immunol. 3:371-382(2003). RN [6] RP FUNCTION, INTERACTION WITH CASP1 AND IL1B, AND TISSUE SPECIFICITY. RX PubMed=15817483; DOI=10.1074/jbc.m410057200; RA Kinoshita T., Wang Y., Hasegawa M., Imamura R., Suda T.; RT "PYPAF3, a PYRIN-containing APAF-1-like protein, is a feedback regulator of RT caspase-1-dependent interleukin-1beta secretion."; RL J. Biol. Chem. 280:21720-21725(2005). RN [7] RP STRUCTURE BY NMR OF 1-96. RX PubMed=20547486; DOI=10.1074/jbc.m110.113191; RA Pinheiro A.S., Proell M., Eibl C., Page R., Schwarzenbacher R., Peti W.; RT "Three-dimensional structure of the NLRP7 pyrin domain: insight into pyrin- RT pyrin-mediated effector domain signaling in innate immunity."; RL J. Biol. Chem. 285:27402-27410(2010). RN [8] RP VARIANTS HYDM1 TRP-693; PRO-693 AND SER-913, AND TISSUE SPECIFICITY. RX PubMed=16462743; DOI=10.1038/ng1740; RA Murdoch S., Djuric U., Mazhar B., Seoud M., Khan R., Kuick R., Bagga R., RA Kircheisen R., Ao A., Ratti B., Hanash S., Rouleau G.A., Slim R.; RT "Mutations in NALP7 cause recurrent hydatidiform moles and reproductive RT wastage in humans."; RL Nat. Genet. 38:300-302(2006). RN [9] RP VARIANTS HYDM1 ARG-398; SER-651; TRP-693; PRO-693; GLN-693; ALA-716; RP TRP-721; TYR-761 AND SER-913. RX PubMed=19246479; DOI=10.1136/jmg.2008.064196; RA Wang C.M., Dixon P.H., Decordova S., Hodges M.D., Sebire N.J., Ozalp S., RA Fallahian M., Sensi A., Ashrafi F., Repiska V., Zhao J., Xiang Y., RA Savage P.M., Seckl M.J., Fisher R.A.; RT "Identification of 13 novel NLRP7 mutations in 20 families with recurrent RT hydatidiform mole; missense mutations cluster in the leucine-rich region."; RL J. Med. Genet. 46:569-575(2009). RN [10] RP VARIANTS HYDM1 ARG-310; ILE-311; ILE-319; ASN-379; THR-481; ARG-511; RP VAL-719 AND THR-799. RX PubMed=23963444; DOI=10.1093/molehr/gat056; RA Andreasen L., Christiansen O.B., Niemann I., Bolund L., Sunde L.; RT "NLRP7 or KHDC3L genes and the etiology of molar pregnancies and recurrent RT miscarriage."; RL Mol. Hum. Reprod. 19:773-781(2013). CC -!- FUNCTION: Inhibits CASP1/caspase-1-dependent IL1B secretion. CC {ECO:0000269|PubMed:15817483}. CC -!- SUBUNIT: Directly interacts with CASP1 and IL1B. CC {ECO:0000269|PubMed:15817483}. CC -!- INTERACTION: CC Q8WX94-3; Q8WX94-3: NLRP7; NbExp=7; IntAct=EBI-21978841, EBI-21978841; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q8WX94-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8WX94-2; Sequence=VSP_016906, VSP_016907; CC Name=3; CC IsoId=Q8WX94-3; Sequence=VSP_016907; CC -!- TISSUE SPECIFICITY: Expressed in numerous tissues including uterus and CC ovary, with low levels in heart and brain. Not detected in skeletal CC muscle. {ECO:0000269|PubMed:15817483, ECO:0000269|PubMed:16462743}. CC -!- INDUCTION: By bacterial lipopolysaccharides (LPS) and IL1B/interleukin- CC 1 beta in peripheral blood mononuclear cells. CC -!- DISEASE: Hydatidiform mole, recurrent, 1 (HYDM1) [MIM:231090]: A CC disorder characterized by excessive trophoblast development that CC produces a growing mass of tissue inside the uterus at the beginning of CC a pregnancy. It leads to abnormal pregnancies with no embryo, and CC cystic degeneration of the chorionic villi. CC {ECO:0000269|PubMed:16462743, ECO:0000269|PubMed:19246479, CC ECO:0000269|PubMed:23963444}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the NLRP family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=INFEVERS; Note=Repertory of FMF and hereditary CC autoinflammatory disorders mutations; CC URL="https://infevers.umai-montpellier.fr/web/search.php?n=8"; 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; AF464765; AAL69963.1; -; mRNA. DR EMBL; AY154462; AAO18158.1; -; mRNA. DR EMBL; AC011476; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC109125; AAI09126.1; -; mRNA. DR EMBL; BK001113; DAA01246.1; -; mRNA. DR CCDS; CCDS12912.1; -. [Q8WX94-2] DR CCDS; CCDS33109.1; -. [Q8WX94-1] DR CCDS; CCDS46183.1; -. [Q8WX94-3] DR RefSeq; NP_001120727.1; NM_001127255.1. [Q8WX94-3] DR RefSeq; NP_631915.2; NM_139176.3. [Q8WX94-2] DR RefSeq; NP_996611.2; NM_206828.3. [Q8WX94-1] DR RefSeq; XP_006723138.1; XM_006723075.3. DR RefSeq; XP_006723139.1; XM_006723076.3. DR RefSeq; XP_011524901.1; XM_011526599.2. DR PDB; 2KM6; NMR; -; A=1-96. DR PDBsum; 2KM6; -. DR AlphaFoldDB; Q8WX94; -. DR BMRB; Q8WX94; -. DR SMR; Q8WX94; -. DR BioGRID; 128265; 162. DR ComplexPortal; CPX-2210; Subcortical maternal complex. DR IntAct; Q8WX94; 7. DR STRING; 9606.ENSP00000467123; -. DR iPTMnet; Q8WX94; -. DR PhosphoSitePlus; Q8WX94; -. DR BioMuta; NLRP7; -. DR DMDM; 24212128; -. DR jPOST; Q8WX94; -. DR MassIVE; Q8WX94; -. DR MaxQB; Q8WX94; -. DR PaxDb; 9606-ENSP00000467123; -. DR PeptideAtlas; Q8WX94; -. DR ProteomicsDB; 74988; -. [Q8WX94-1] DR ProteomicsDB; 74989; -. [Q8WX94-2] DR ProteomicsDB; 74990; -. [Q8WX94-3] DR Antibodypedia; 46386; 186 antibodies from 28 providers. DR DNASU; 199713; -. DR Ensembl; ENST00000328092.9; ENSP00000329568.5; ENSG00000167634.12. [Q8WX94-2] DR Ensembl; ENST00000340844.6; ENSP00000339491.2; ENSG00000167634.12. [Q8WX94-1] DR Ensembl; ENST00000588756.5; ENSP00000467123.1; ENSG00000167634.12. [Q8WX94-3] DR Ensembl; ENST00000590030.5; ENSP00000465520.1; ENSG00000167634.12. [Q8WX94-1] DR Ensembl; ENST00000592784.6; ENSP00000468706.1; ENSG00000167634.12. [Q8WX94-3] DR Ensembl; ENST00000610424.4; ENSP00000482887.1; ENSG00000274571.4. [Q8WX94-3] DR Ensembl; ENST00000610790.1; ENSP00000478726.1; ENSG00000274571.4. [Q8WX94-1] DR Ensembl; ENST00000610853.4; ENSP00000478890.1; ENSG00000274571.4. [Q8WX94-2] DR Ensembl; ENST00000610981.4; ENSP00000479459.1; ENSG00000277776.4. [Q8WX94-3] DR Ensembl; ENST00000611597.4; ENSP00000481117.1; ENSG00000274571.4. [Q8WX94-1] DR Ensembl; ENST00000613233.1; ENSP00000483203.1; ENSG00000277776.4. [Q8WX94-1] DR Ensembl; ENST00000614879.1; ENSP00000484444.1; ENSG00000277071.4. [Q8WX94-1] DR Ensembl; ENST00000615426.4; ENSP00000484426.1; ENSG00000277071.4. [Q8WX94-3] DR Ensembl; ENST00000615699.1; ENSP00000480449.1; ENSG00000277786.4. [Q8WX94-1] DR Ensembl; ENST00000618261.1; ENSP00000483353.1; ENSG00000277179.4. [Q8WX94-1] DR Ensembl; ENST00000618343.4; ENSP00000480226.1; ENSG00000274174.4. [Q8WX94-3] DR Ensembl; ENST00000618672.4; ENSP00000481452.1; ENSG00000277179.4. [Q8WX94-3] DR Ensembl; ENST00000618740.4; ENSP00000484808.1; ENSG00000277786.4. [Q8WX94-3] DR Ensembl; ENST00000618995.1; ENSP00000481809.1; ENSG00000276804.4. [Q8WX94-1] DR Ensembl; ENST00000620183.1; ENSP00000480034.1; ENSG00000274174.4. [Q8WX94-1] DR Ensembl; ENST00000620820.4; ENSP00000482551.1; ENSG00000276804.4. [Q8WX94-3] DR Ensembl; ENST00000621238.4; ENSP00000481395.1; ENSG00000274571.4. [Q8WX94-3] DR Ensembl; ENST00000621584.1; ENSP00000479541.1; ENSG00000275483.4. [Q8WX94-1] DR Ensembl; ENST00000622199.4; ENSP00000482194.1; ENSG00000275483.4. [Q8WX94-3] DR GeneID; 199713; -. DR KEGG; hsa:199713; -. DR MANE-Select; ENST00000592784.6; ENSP00000468706.1; NM_001127255.2; NP_001120727.1. [Q8WX94-3] DR UCSC; uc002qih.4; human. [Q8WX94-1] DR AGR; HGNC:22947; -. DR CTD; 199713; -. DR DisGeNET; 199713; -. DR GeneCards; NLRP7; -. DR HGNC; HGNC:22947; NLRP7. DR HPA; ENSG00000167634; Tissue enriched (testis). DR MalaCards; NLRP7; -. DR MIM; 231090; phenotype. DR MIM; 609661; gene. DR neXtProt; NX_Q8WX94; -. DR OpenTargets; ENSG00000167634; -. DR Orphanet; 254688; Complete hydatidiform mole. DR Orphanet; 254693; Partial hydatidiform mole. DR PharmGKB; PA162398003; -. DR VEuPathDB; HostDB:ENSG00000167634; -. DR eggNOG; ENOG502S92U; Eukaryota. DR GeneTree; ENSGT00940000164627; -. DR HOGENOM; CLU_002274_2_1_1; -. DR InParanoid; Q8WX94; -. DR OMA; QNYLEHL; -. DR OrthoDB; 55870at2759; -. DR PhylomeDB; Q8WX94; -. DR PathwayCommons; Q8WX94; -. DR SignaLink; Q8WX94; -. DR BioGRID-ORCS; 199713; 11 hits in 1140 CRISPR screens. DR EvolutionaryTrace; Q8WX94; -. DR GeneWiki; NLRP7; -. DR GenomeRNAi; 199713; -. DR Pharos; Q8WX94; Tbio. DR PRO; PR:Q8WX94; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; Q8WX94; Protein. DR Bgee; ENSG00000167634; Expressed in primordial germ cell in gonad and 37 other cell types or tissues. DR ExpressionAtlas; Q8WX94; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0019828; F:aspartic-type endopeptidase inhibitor activity; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0089720; F:caspase binding; IPI:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0019966; F:interleukin-1 binding; IPI:UniProtKB. DR GO; GO:0071347; P:cellular response to interleukin-1; IEP:UniProtKB. DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEP:UniProtKB. DR GO; GO:1900016; P:negative regulation of cytokine production involved in inflammatory response; IMP:UniProtKB. DR GO; GO:0032691; P:negative regulation of interleukin-1 beta production; IMP:UniProtKB. DR GO; GO:0010955; P:negative regulation of protein processing; IDA:UniProtKB. DR GO; GO:0050727; P:regulation of inflammatory response; IBA:GO_Central. DR CDD; cd08320; Pyrin_NALPs; 1. DR Gene3D; 1.10.533.10; Death Domain, Fas; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1. DR InterPro; IPR004020; DAPIN. DR InterPro; IPR011029; DEATH-like_dom_sf. DR InterPro; IPR001611; Leu-rich_rpt. DR InterPro; IPR032675; LRR_dom_sf. DR InterPro; IPR007111; NACHT_NTPase. DR InterPro; IPR041267; NLRP_HD2. DR InterPro; IPR041075; NOD2_WH. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR45690; NACHT, LRR AND PYD DOMAINS-CONTAINING PROTEIN 12; 1. DR PANTHER; PTHR45690:SF20; NACHT, LRR AND PYD DOMAINS-CONTAINING PROTEIN 7; 1. DR Pfam; PF13516; LRR_6; 2. DR Pfam; PF05729; NACHT; 1. DR Pfam; PF17776; NLRC4_HD2; 1. DR Pfam; PF17779; NOD2_WH; 1. DR Pfam; PF02758; PYRIN; 1. DR SMART; SM00368; LRR_RI; 5. DR SMART; SM01289; PYRIN; 1. DR SUPFAM; SSF47986; DEATH domain; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF52047; RNI-like; 1. DR PROSITE; PS50824; DAPIN; 1. DR PROSITE; PS50837; NACHT; 1. DR Genevisible; Q8WX94; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; ATP-binding; Disease variant; KW Leucine-rich repeat; Nucleotide-binding; Reference proteome; Repeat. FT CHAIN 1..980 FT /note="NACHT, LRR and PYD domains-containing protein 7" FT /id="PRO_0000080895" FT DOMAIN 1..93 FT /note="Pyrin" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00061" FT DOMAIN 172..491 FT /note="NACHT" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00136" FT REPEAT 614..638 FT /note="LRR 1" FT REPEAT 674..697 FT /note="LRR 2" FT REPEAT 760..784 FT /note="LRR 3" FT REPEAT 788..810 FT /note="LRR 4" FT REPEAT 817..840 FT /note="LRR 5" FT REPEAT 845..868 FT /note="LRR 6" FT REPEAT 874..897 FT /note="LRR 7" FT REPEAT 902..928 FT /note="LRR 8" FT REPEAT 933..957 FT /note="LRR 9" FT REGION 104..123 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 109..123 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 178..185 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00136" FT VAR_SEQ 644..671 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_016906" FT VAR_SEQ 938 FT /note="L -> LWSCSLMPFYCQHLGSALLSNQKLETLDLGQNHLWKSGIIKLFGVLR FT QRTGSLKILRL (in isoform 2 and isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_016907" FT VARIANT 310 FT /note="Q -> R (in HYDM1; uncertain significance; FT dbSNP:rs77812009)" FT /evidence="ECO:0000269|PubMed:23963444" FT /id="VAR_085072" FT VARIANT 311 FT /note="L -> I (in HYDM1; uncertain significance; FT dbSNP:rs79513034)" FT /evidence="ECO:0000269|PubMed:23963444" FT /id="VAR_085073" FT VARIANT 319 FT /note="V -> I (in HYDM1; uncertain significance; FT dbSNP:rs775882)" FT /evidence="ECO:0000269|PubMed:23963444" FT /id="VAR_026710" FT VARIANT 379 FT /note="K -> N (in HYDM1; uncertain significance; FT dbSNP:rs10418277)" FT /evidence="ECO:0000269|PubMed:23963444" FT /id="VAR_085074" FT VARIANT 398 FT /note="L -> R (in HYDM1; dbSNP:rs104895548)" FT /evidence="ECO:0000269|PubMed:19246479" FT /id="VAR_059035" FT VARIANT 481 FT /note="A -> T (in HYDM1; uncertain significance; FT dbSNP:rs61747414)" FT /evidence="ECO:0000269|PubMed:23963444" FT /id="VAR_085075" FT VARIANT 487 FT /note="G -> E (in dbSNP:rs775881)" FT /id="VAR_060103" FT VARIANT 511 FT /note="K -> R (in HYDM1; uncertain significance; FT dbSNP:rs61743949)" FT /evidence="ECO:0000269|PubMed:23963444" FT /id="VAR_085076" FT VARIANT 651 FT /note="P -> S (in HYDM1; dbSNP:rs104895549)" FT /evidence="ECO:0000269|PubMed:19246479" FT /id="VAR_059036" FT VARIANT 693 FT /note="R -> P (in HYDM1; dbSNP:rs104895502)" FT /evidence="ECO:0000269|PubMed:16462743, FT ECO:0000269|PubMed:19246479" FT /id="VAR_026711" FT VARIANT 693 FT /note="R -> Q (in HYDM1; dbSNP:rs104895502)" FT /evidence="ECO:0000269|PubMed:19246479" FT /id="VAR_059037" FT VARIANT 693 FT /note="R -> W (in HYDM1; dbSNP:rs104895506)" FT /evidence="ECO:0000269|PubMed:16462743, FT ECO:0000269|PubMed:19246479" FT /id="VAR_026712" FT VARIANT 716 FT /note="P -> A (in HYDM1; dbSNP:rs104895550)" FT /evidence="ECO:0000269|PubMed:19246479" FT /id="VAR_059038" FT VARIANT 719 FT /note="A -> V (in HYDM1; uncertain significance; FT dbSNP:rs104895526)" FT /evidence="ECO:0000269|PubMed:23963444" FT /id="VAR_085077" FT VARIANT 721 FT /note="R -> W (in HYDM1; dbSNP:rs104895525)" FT /evidence="ECO:0000269|PubMed:19246479" FT /id="VAR_059039" FT VARIANT 761 FT /note="C -> Y (in HYDM1; dbSNP:rs104895552)" FT /evidence="ECO:0000269|PubMed:19246479" FT /id="VAR_059040" FT VARIANT 799 FT /note="N -> T (in HYDM1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:23963444" FT /id="VAR_085078" FT VARIANT 913 FT /note="N -> S (in HYDM1; dbSNP:rs104895503)" FT /evidence="ECO:0000269|PubMed:16462743, FT ECO:0000269|PubMed:19246479" FT /id="VAR_026713" FT VARIANT 971 FT /note="T -> A (in dbSNP:rs7256020)" FT /id="VAR_026714" FT CONFLICT 310..311 FT /note="QL -> RI (in Ref. 4; AAI09126)" FT /evidence="ECO:0000305" FT CONFLICT 481 FT /note="A -> T (in Ref. 4; AAI09126)" FT /evidence="ECO:0000305" FT HELIX 4..16 FT /evidence="ECO:0007829|PDB:2KM6" FT HELIX 21..29 FT /evidence="ECO:0007829|PDB:2KM6" FT HELIX 38..40 FT /evidence="ECO:0007829|PDB:2KM6" FT HELIX 43..48 FT /evidence="ECO:0007829|PDB:2KM6" FT HELIX 52..61 FT /evidence="ECO:0007829|PDB:2KM6" FT HELIX 64..77 FT /evidence="ECO:0007829|PDB:2KM6" FT HELIX 84..87 FT /evidence="ECO:0007829|PDB:2KM6" FT TURN 88..91 FT /evidence="ECO:0007829|PDB:2KM6" SQ SEQUENCE 980 AA; 111807 MW; 822AF2FD4338003D CRC64; MTSPQLEWTL QTLLEQLNED ELKSFKSLLW AFPLEDVLQK TPWSEVEEAD GKKLAEILVN TSSENWIRNA TVNILEEMNL TELCKMAKAE MMEDGQVQEI DNPELGDAEE DSELAKPGEK EGWRNSMEKQ SLVWKNTFWQ GDIDNFHDDV TLRNQRFIPF LNPRTPRKLT PYTVVLHGPA GVGKTTLAKK CMLDWTDCNL SPTLRYAFYL SCKELSRMGP CSFAELISKD WPELQDDIPS ILAQAQRILF VVDGLDELKV PPGALIQDIC GDWEKKKPVP VLLGSLLKRK MLPRAALLVT TRPRALRDLQ LLAQQPIYVR VEGFLEEDRR AYFLRHFGDE DQAMRAFELM RSNAALFQLG SAPAVCWIVC TTLKLQMEKG EDPVPTCLTR TGLFLRFLCS RFPQGAQLRG ALRTLSLLAA QGLWAQMSVF HREDLERLGV QESDLRLFLD GDILRQDRVS KGCYSFIHLS FQQFLTALFY ALEKEEGEDR DGHAWDIGDV QKLLSGEERL KNPDLIQVGH FLFGLANEKR AKELEATFGC RMSPDIKQEL LQCKAHLHAN KPLSVTDLKE VLGCLYESQE EELAKVVVAP FKEISIHLTN TSEVMHCSFS LKHCQDLQKL SLQVAKGVFL ENYMDFELDI EFERCTYLTI PNWARQDLRS LRLWTDFCSL FSSNSNLKFL EVKQSFLSDS SVRILCDHVT RSTCHLQKVE IKNVTPDTAY RDFCLAFIGK KTLTHLTLAG HIEWERTMML MLCDLLRNHK CNLQYLRLGG HCATPEQWAE FFYVLKANQS LKHLRLSANV LLDEGAMLLY KTMTRPKHFL QMLSLENCRL TEASCKDLAA VLVVSKKLTH LCLAKNPIGD TGVKFLCEGL SYPDCKLQTL VLQQCSITKL GCRYLSEALQ EACSLTNLDL SINQIARGLW ILCQALENPN CNLKHLRLKT YETNLEIKKL LEEVKEKNPK LTIDCNASGA TAPPCCDFFC //