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NALP7_HUMAN
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   03-AUG-2022, entry version 173.
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";
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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. [Q8WX94-3]
DR   RefSeq; XP_006723139.1; XM_006723076.3. [Q8WX94-3]
DR   RefSeq; XP_011524901.1; XM_011526599.2. [Q8WX94-3]
DR   PDB; 2KM6; NMR; -; A=1-96.
DR   PDBsum; 2KM6; -.
DR   AlphaFoldDB; Q8WX94; -.
DR   BMRB; Q8WX94; -.
DR   SMR; Q8WX94; -.
DR   BioGRID; 128265; 162.
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   PeptideAtlas; Q8WX94; -.
DR   PRIDE; Q8WX94; -.
DR   ProteomicsDB; 74988; -. [Q8WX94-1]
DR   ProteomicsDB; 74989; -. [Q8WX94-2]
DR   ProteomicsDB; 74990; -. [Q8WX94-3]
DR   Antibodypedia; 46386; 161 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; ENST00000592784.5; 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   UCSC; uc002qih.4; human. [Q8WX94-1]
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; CCEIVVS; -.
DR   OrthoDB; 155336at2759; -.
DR   PhylomeDB; Q8WX94; -.
DR   PathwayCommons; Q8WX94; -.
DR   SignaLink; Q8WX94; -.
DR   BioGRID-ORCS; 199713; 11 hits in 1062 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 granulocyte and 36 other tissues.
DR   ExpressionAtlas; Q8WX94; baseline and differential.
DR   Genevisible; Q8WX94; HS.
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:1905246; P:negative regulation of aspartic-type peptidase activity; IDA: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   Gene3D; 1.10.533.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   Gene3D; 3.80.10.10; -; 1.
DR   InterPro; IPR004020; DAPIN.
DR   InterPro; IPR011029; DEATH-like_dom_sf.
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   Pfam; PF05729; NACHT; 1.
DR   Pfam; PF17776; NLRC4_HD2; 1.
DR   Pfam; PF17779; NOD2_WH; 1.
DR   Pfam; PF02758; PYRIN; 1.
DR   SMART; SM01289; PYRIN; 1.
DR   SUPFAM; SSF47986; SSF47986; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS50824; DAPIN; 1.
DR   PROSITE; PS50837; NACHT; 1.
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; unknown pathological significance;
FT                   dbSNP:rs77812009)"
FT                   /evidence="ECO:0000269|PubMed:23963444"
FT                   /id="VAR_085072"
FT   VARIANT         311
FT                   /note="L -> I (in HYDM1; unknown pathological significance;
FT                   dbSNP:rs79513034)"
FT                   /evidence="ECO:0000269|PubMed:23963444"
FT                   /id="VAR_085073"
FT   VARIANT         319
FT                   /note="V -> I (in HYDM1; unknown pathological significance;
FT                   dbSNP:rs775882)"
FT                   /evidence="ECO:0000269|PubMed:23963444"
FT                   /id="VAR_026710"
FT   VARIANT         379
FT                   /note="K -> N (in HYDM1; unknown pathological 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; unknown pathological 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; unknown pathological 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; unknown pathological 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; unknown pathological
FT                   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
 
 
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