ZNFX1_HUMAN
ID ZNFX1_HUMAN Reviewed; 1918 AA.
AC Q9P2E3; Q9BQM7; Q9BQM8; Q9H8C1; Q9H9S2; Q9NUM1; Q9NWW1;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=NFX1-type zinc finger-containing protein 1 {ECO:0000305};
GN Name=ZNFX1 {ECO:0000303|PubMed:33872655, ECO:0000312|HGNC:HGNC:29271};
GN Synonyms=KIAA1404 {ECO:0000303|PubMed:10718198};
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 [LARGE SCALE MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP VARIANTS HIS-924 AND ILE-1351.
RC TISSUE=Brain;
RX PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVI. The
RT complete sequences of 150 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:65-73(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP HIS-924.
RC TISSUE=Neuron, and Placenta;
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 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 [4]
RP INVOLVEMENT IN IMD91, FUNCTION, TISSUE SPECIFICITY, AND VARIANTS IMD91
RP 133-LYS--MET-1918 DEL; GLN-377; PRO-1051; THR-1154; SER-1264 AND SER-1292.
RX PubMed=33872655; DOI=10.1016/j.jaci.2021.03.045;
RA Vavassori S., Chou J., Faletti L.E., Haunerdinger V., Opitz L., Joset P.,
RA Fraser C.J., Prader S., Gao X., Schuch L.A., Wagner M., Hoefele J.,
RA Maccari M.E., Zhu Y., Elakis G., Gabbett M.T., Forstner M., Omran H.,
RA Kaiser T., Kessler C., Olbrich H., Frosk P., Almutairi A., Platt C.D.,
RA Elkins M., Weeks S., Rubin T., Planas R., Marchetti T., Koovely D.,
RA Klaembt V., Soliman N.A., von Hardenberg S., Klemann C., Baumann U.,
RA Lenz D., Klein-Franke A., Schwemmle M., Huber M., Sturm E., Hartleif S.,
RA Haeffner K., Gimpel C., Brotschi B., Laube G., Guengoer T., Buckley M.F.,
RA Kottke R., Staufner C., Hildebrandt F., Reu-Hofer S., Moll S., Weber A.,
RA Kaur H., Ehl S., Hiller S., Geha R., Roscioli T., Griese M.,
RA Pachlopnik Schmid J.;
RT "Multisystem inflammation and susceptibility to viral infections in human
RT ZNFX1 deficiency.";
RL J. Allergy Clin. Immunol. 148:381-393(2021).
RN [5]
RP RZ-TYPE ZINC-FINGER.
RX PubMed=34012115; DOI=10.1038/s41586-021-03566-4;
RA Otten E.G., Werner E., Crespillo-Casado A., Boyle K.B., Dharamdasani V.,
RA Pathe C., Santhanam B., Randow F.;
RT "Ubiquitylation of lipopolysaccharide by RNF213 during bacterial
RT infection.";
RL Nature 594:111-116(2021).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, INVOLVEMENT IN IMD91, AND VARIANT IMD91
RP 959-SER--MET-1918 DEL.
RX PubMed=33876776; DOI=10.1073/pnas.2102804118;
RA Le Voyer T., Neehus A.L., Yang R., Ogishi M., Rosain J., Alroqi F.,
RA Alshalan M., Blumental S., Al Ali F., Khan T., Ata M., Rozen L.,
RA Demulder A., Bastard P., Gruber C., Roynard M., Seeleuthener Y.,
RA Rapaport F., Bigio B., Chrabieh M., Sng D., Berteloot L., Boddaert N.,
RA Rozenberg F., Al-Muhsen S., Bertoli-Avella A., Abel L., Bogunovic D.,
RA Marr N., Mansouri D., Al Mutairi F., Beziat V., Weil D., Mahdaviani S.A.,
RA Ferster A., Zhang S.Y., Reversade B., Boisson-Dupuis S., Casanova J.L.,
RA Bustamante J.;
RT "Inherited deficiency of stress granule ZNFX1 in patients with monocytosis
RT and mycobacterial disease.";
RL Proc. Natl. Acad. Sci. U.S.A. 118:0-0(2021).
CC -!- FUNCTION: RNA-binding protein that initiates the antiviral response and
CC is required to restrict the replication of RNA viruses
CC (PubMed:33872655). Acts as a double-stranded RNA (dsRNA) sensor that
CC recognizes viral RNA and then interacts with MAVS to initiate the type
CC I interferon response (By similarity). Also required for immunity
CC against some bacteria, such as mycobacteria (PubMed:33876776).
CC {ECO:0000250|UniProtKB:Q8R151, ECO:0000269|PubMed:33872655,
CC ECO:0000269|PubMed:33876776}.
CC -!- SUBUNIT: Interacts with MAVS. {ECO:0000250|UniProtKB:Q8R151}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:Q8R151}. Cytoplasm, Stress granule
CC {ECO:0000269|PubMed:33876776}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9P2E3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9P2E3-2; Sequence=VSP_002434, VSP_002435;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10718198,
CC ECO:0000269|PubMed:33872655}.
CC -!- DISEASE: Immunodeficiency 91 and hyperinflammation (IMD91)
CC [MIM:619644]: An autosomal recessive disorder characterized by
CC immunodeficiency, recurrent infections, and hyperinflammation with
CC systemic involvement. Most patients eventually develop hepatic or renal
CC failure, may have compromised neurologic function, lymphadenopathy or
CC hepatosplenomegaly. Early death often occurs due to multiorgan failure.
CC {ECO:0000269|PubMed:33872655, ECO:0000269|PubMed:33876776}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the ZNFX1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91264.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA92642.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB14149.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB14696.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB037825; BAA92642.1; ALT_INIT; mRNA.
DR EMBL; AK000573; BAA91264.1; ALT_INIT; mRNA.
DR EMBL; AK002139; BAA92102.1; -; mRNA.
DR EMBL; AK022641; BAB14149.1; ALT_INIT; mRNA.
DR EMBL; AK023836; BAB14696.1; ALT_SEQ; mRNA.
DR EMBL; AL049766; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS13417.1; -. [Q9P2E3-1]
DR RefSeq; NP_066363.1; NM_021035.2. [Q9P2E3-1]
DR RefSeq; XP_006723899.1; XM_006723836.1.
DR AlphaFoldDB; Q9P2E3; -.
DR SMR; Q9P2E3; -.
DR BioGRID; 121422; 59.
DR IntAct; Q9P2E3; 31.
DR MINT; Q9P2E3; -.
DR STRING; 9606.ENSP00000379412; -.
DR iPTMnet; Q9P2E3; -.
DR MetOSite; Q9P2E3; -.
DR PhosphoSitePlus; Q9P2E3; -.
DR BioMuta; ZNFX1; -.
DR DMDM; 23821814; -.
DR EPD; Q9P2E3; -.
DR jPOST; Q9P2E3; -.
DR MassIVE; Q9P2E3; -.
DR MaxQB; Q9P2E3; -.
DR PaxDb; Q9P2E3; -.
DR PeptideAtlas; Q9P2E3; -.
DR PRIDE; Q9P2E3; -.
DR ProteomicsDB; 83792; -. [Q9P2E3-1]
DR ProteomicsDB; 83793; -. [Q9P2E3-2]
DR Antibodypedia; 28464; 25 antibodies from 8 providers.
DR DNASU; 57169; -.
DR Ensembl; ENST00000371752.5; ENSP00000360817.1; ENSG00000124201.15. [Q9P2E3-1]
DR Ensembl; ENST00000396105.6; ENSP00000379412.1; ENSG00000124201.15. [Q9P2E3-1]
DR GeneID; 57169; -.
DR KEGG; hsa:57169; -.
DR MANE-Select; ENST00000396105.6; ENSP00000379412.1; NM_021035.3; NP_066363.1.
DR UCSC; uc002xui.5; human. [Q9P2E3-1]
DR CTD; 57169; -.
DR DisGeNET; 57169; -.
DR GeneCards; ZNFX1; -.
DR HGNC; HGNC:29271; ZNFX1.
DR HPA; ENSG00000124201; Low tissue specificity.
DR MIM; 618931; gene.
DR MIM; 619644; phenotype.
DR neXtProt; NX_Q9P2E3; -.
DR OpenTargets; ENSG00000124201; -.
DR PharmGKB; PA143485687; -.
DR VEuPathDB; HostDB:ENSG00000124201; -.
DR eggNOG; KOG1807; Eukaryota.
DR GeneTree; ENSGT00940000155154; -.
DR HOGENOM; CLU_001066_0_1_1; -.
DR InParanoid; Q9P2E3; -.
DR OMA; CIGNMGM; -.
DR OrthoDB; 271662at2759; -.
DR PhylomeDB; Q9P2E3; -.
DR TreeFam; TF323611; -.
DR PathwayCommons; Q9P2E3; -.
DR SignaLink; Q9P2E3; -.
DR BioGRID-ORCS; 57169; 21 hits in 1086 CRISPR screens.
DR ChiTaRS; ZNFX1; human.
DR GenomeRNAi; 57169; -.
DR Pharos; Q9P2E3; Tdark.
DR PRO; PR:Q9P2E3; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q9P2E3; protein.
DR Bgee; ENSG00000124201; Expressed in cardiac muscle of right atrium and 190 other tissues.
DR ExpressionAtlas; Q9P2E3; baseline and differential.
DR Genevisible; Q9P2E3; HS.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:UniProtKB.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR GO; GO:0031380; C:nuclear RNA-directed RNA polymerase complex; IBA:GO_Central.
DR GO; GO:0004386; F:helicase activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0002218; P:activation of innate immune response; ISS:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
DR GO; GO:0051607; P:defense response to virus; IMP:UniProtKB.
DR GO; GO:0031048; P:heterochromatin assembly by small RNA; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0045071; P:negative regulation of viral genome replication; ISS:UniProtKB.
DR CDD; cd18808; SF1_C_Upf1; 1.
DR Gene3D; 3.40.50.300; -; 3.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR045055; DNA2/NAM7-like.
DR InterPro; IPR041679; DNA2/NAM7-like_C.
DR InterPro; IPR041677; DNA2/NAM7_AAA_11.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000967; Znf_NFX1.
DR PANTHER; PTHR10887; PTHR10887; 2.
DR Pfam; PF13086; AAA_11; 1.
DR Pfam; PF13087; AAA_12; 1.
DR SMART; SM00438; ZnF_NFX; 5.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51981; ZF_RZ; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Antiviral defense; Coiled coil; Cytoplasm;
KW Disease variant; Immunity; Innate immunity; Membrane; Metal-binding;
KW Mitochondrion; Mitochondrion outer membrane; Reference proteome; Repeat;
KW RNA-binding; Zinc; Zinc-finger.
FT CHAIN 1..1918
FT /note="NFX1-type zinc finger-containing protein 1"
FT /id="PRO_0000050795"
FT ZN_FING 1298..1320
FT /note="NF-X1-type 1"
FT ZN_FING 1330..1346
FT /note="NF-X1-type 2"
FT ZN_FING 1382..1400
FT /note="NF-X1-type 3"
FT ZN_FING 1441..1463
FT /note="NF-X1-type 4"
FT ZN_FING 1471..1488
FT /note="NF-X1-type 5"
FT ZN_FING 1546..1564
FT /note="NF-X1-type 6"
FT ZN_FING 1827..1898
FT /note="RZ-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01325,
FT ECO:0000303|PubMed:34012115"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 75..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 796..819
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 876..896
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 286..313
FT /evidence="ECO:0000255"
FT COILED 886..967
FT /evidence="ECO:0000255"
FT COILED 1741..1820
FT /evidence="ECO:0000255"
FT COMPBIAS 1..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1849
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01325"
FT BINDING 1853
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01325"
FT BINDING 1869
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01325"
FT BINDING 1872
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01325"
FT VAR_SEQ 890..903
FT /note="QRNQKKKMKKRVKD -> VPCLVLMSADPAQP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_002434"
FT VAR_SEQ 904..1918
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_002435"
FT VARIANT 133..1918
FT /note="Missing (in IMD91)"
FT /evidence="ECO:0000269|PubMed:33872655"
FT /id="VAR_085313"
FT VARIANT 377
FT /note="R -> Q (in IMD91; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:33872655"
FT /id="VAR_085314"
FT VARIANT 864
FT /note="L -> V (in dbSNP:rs2664578)"
FT /id="VAR_014078"
FT VARIANT 910
FT /note="T -> A (in dbSNP:rs2273148)"
FT /id="VAR_014079"
FT VARIANT 924
FT /note="Q -> H (in dbSNP:rs238221)"
FT /evidence="ECO:0000269|PubMed:10718198,
FT ECO:0000269|PubMed:14702039"
FT /id="VAR_014080"
FT VARIANT 959..1918
FT /note="Missing (in IMD91)"
FT /evidence="ECO:0000269|PubMed:33876776"
FT /id="VAR_085315"
FT VARIANT 1051
FT /note="L -> P (in IMD91; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:33872655"
FT /id="VAR_085316"
FT VARIANT 1154
FT /note="I -> T (in IMD91; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:33872655"
FT /id="VAR_085317"
FT VARIANT 1259
FT /note="M -> I (in dbSNP:rs6512577)"
FT /id="VAR_024487"
FT VARIANT 1264
FT /note="C -> S (in IMD91; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:33872655"
FT /id="VAR_085318"
FT VARIANT 1292
FT /note="C -> S (in IMD91; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:33872655"
FT /id="VAR_085319"
FT VARIANT 1297
FT /note="G -> S (in dbSNP:rs36068952)"
FT /id="VAR_051504"
FT VARIANT 1351
FT /note="T -> I (in dbSNP:rs238209)"
FT /evidence="ECO:0000269|PubMed:10718198"
FT /id="VAR_014081"
FT CONFLICT 738
FT /note="C -> S (in Ref. 2; BAB14696)"
FT /evidence="ECO:0000305"
FT CONFLICT 755
FT /note="P -> L (in Ref. 2; BAA92102)"
FT /evidence="ECO:0000305"
FT CONFLICT 891
FT /note="R -> H (in Ref. 2; BAB14696)"
FT /evidence="ECO:0000305"
FT CONFLICT 1715
FT /note="L -> P (in Ref. 2; BAB14696)"
FT /evidence="ECO:0000305"
FT CONFLICT 1743
FT /note="K -> Q (in Ref. 2; BAA91264)"
FT /evidence="ECO:0000305"
FT CONFLICT 1773
FT /note="Y -> N (in Ref. 2; BAB14696)"
FT /evidence="ECO:0000305"
FT CONFLICT 1856
FT /note="V -> E (in Ref. 2; BAB14696)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1918 AA; 220227 MW; 4E6F2C193BC313CE CRC64;
MEERRPHLDA RPRNSHTNHR GPVDGELPPR ARNQANNPPA NALRGGASHP GRHPRANNHP
AAYWQREERF RAMGRNPHQG RRNQEGHASD EARDQRHDQE NDTRWRNGNQ DCRNRRPPWS
NDNFQQWRTP HQKPTEQPQQ AKKLGYKFLE SLLQKDPSEV VITLATSLGL KELLSHSSMK
SNFLELICQV LRKACSSKMD RQSVLHVLGI LKNSKFLKVC LPAYVVGMIT EPIPDIRNQY
PEHISNIISL LQDLVSVFPA SSVQETSMLV SLLPTSLNAL RASGVDIEEE TEKNLEKVQT
IIEHLQEKRR EGTLRVDTYT LVQPEAEDHV ESYRTMPIYP TYNEVHLDER PFLRPNIISG
KYDSTAIYLD THFRLLREDF VRPLREGILE LLQSFEDQGL RKRKFDDIRI YFDTRIITPM
CSSSGIVYKV QFDTKPLKFV RWQNSKRLLY GSLVCMSKDN FETFLFATVS NREQEDLCRG
IVQLCFNEQS QQLLAEVQPS DSFLMVETTA YFEAYRHVLE GLQEVQEEDV PFQRNIVECN
SHVKEPRYLL MGGRYDFTPL IENPSATGEF LRNVEGLRHP RINVLDPGQW PSKEALKLDD
SQMEALQFAL TRELAIIQGP PGTGKTYVGL KIVQALLTNE SVWQISLQKF PILVVCYTNH
ALDQFLEGIY NCQKTSIVRV GGRSNSEILK QFTLRELRNK REFRRNLPMH LRRAYMSIMT
QMKESEQELH EGAKTLECTM RGVLREQYLQ KYISPQHWES LMNGPVQDSE WICFQHWKHS
MMLEWLGLGV GSFTQSVSPA GPENTAQAEG DEEEEGEEES SLIEIAEEAD LIQADRVIEE
EEVVRPQRRK KEESGADQEL AKMLLAMRLD HCGTGTAAGQ EQATGEWQTQ RNQKKKMKKR
VKDELRKLNT MTAAEANEIE DVWQLDLSSR WQLYRLWLQL YQADTRRKIL SYERQYRTSA
ERMAELRLQE DLHILKDAQV VGMTTTGAAK YRQILQKVEP RIVIVEEAAE VLEAHTIATL
SKACQHLILI GDHQQLRPSA NVYDLAKNFN LEVSLFERLV KVNIPFVRLN YQHRMCPEIA
RLLTPHIYQD LENHPSVLKY EKIKGVSSNL FFVEHNFPEQ EIQEGKSHQN QHEAHFVVEL
CKYFLCQEYL PSQITILTTY TGQLFCLRKL MPAKTFAGVR VHVVDKYQGE ENDIILLSLV
RSNQEGKVGF LQISNRICVA LSRAKKGMYC IGNMQMLAKV PLWSKIIHTL RENNQIGPML
RLCCQNHPET HTLVSKASDF QKVPEGGCSL PCEFRLGCGH VCTRACHPYD SSHKEFQCMK
PCQKVICQEG HRCPLVCFQE CQPCQVKVPK TIPRCGHEQM VPCSVPESDF CCQEPCSKSL
RCGHRCSHPC GEDCVQLCSE MVTIKLKCGH SQPVKCGHVE GLLYGGLLVK CTTKCGTILD
CGHPCPGSCH SCFEGRFHER CQQPCKRLLI CSHKCQEPCI GECPPCQRTC QNRCVHSQCK
KKCGELCSPC VEPCVWRCQH YQCTKLCSEP CNRPPCYVPC TKLLVCGHPC IGLCGEPCPK
KCRICHMDEV TQIFFGFEDE PDARFVQLED CSHIFEVQAL DRYMNEQKDD EVAIRLKVCP
ICQVPIRKNL RYGTSIKQRL EEIEIIKEKI QGSAGEIATS QERLKALLER KSLLHQLLPE
DFLMLKEKLA QKNLSVKDLG LVENYISFYD HLASLWDSLK KMHVLEEKRV RTRLEQVHEW
LAKKRLSFTS QELSDLRSEI QRLTYLVNLL TRYKIAEKKV KDSIAVEVYS VQNILEKTCK
FTQEDEQLVQ EKMEALKATL PCSGLGISEE ERVQIVSAIG YPRGHWFKCR NGHIYVIGDC
GGAMERGTCP DCKEVIGGTN HTLERSNQLA SEMDGAQHAA WSDTANNLMN FEEIQGMM
