ZEP3_HUMAN
ID ZEP3_HUMAN Reviewed; 2406 AA.
AC Q5T1R4; A7YY91; Q5T1R5; Q9BZS0; Q9HCL7;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Transcription factor HIVEP3;
DE AltName: Full=Human immunodeficiency virus type I enhancer-binding protein 3;
DE AltName: Full=Kappa-B and V(D)J recombination signal sequences-binding protein;
DE AltName: Full=Kappa-binding protein 1;
DE Short=KBP-1;
DE AltName: Full=Zinc finger protein ZAS3;
GN Name=HIVEP3; Synonyms=KBP1, KIAA1555, KRC, ZAS3;
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), FUNCTION, ALTERNATIVE SPLICING,
RP DOMAIN, AND VARIANTS ARG-575; PRO-2023; ALA-2109; ARG-2272 AND ALA-2339.
RC TISSUE=Brain;
RX PubMed=11161801; DOI=10.1006/geno.2000.6425;
RA Hicar M.D., Liu Y., Allen C.E., Wu L.-C.;
RT "Structure of the human zinc finger protein HIVEP3: molecular cloning,
RT expression, exon-intron structure, and comparison with paralogous genes
RT HIVEP1 and HIVEP2.";
RL Genomics 71:89-100(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS ARG-575;
RP PRO-2023; ALA-2109 AND ALA-2339.
RC TISSUE=Brain;
RX PubMed=10997877; DOI=10.1093/dnares/7.4.271;
RA Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:273-281(2000).
RN [3]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS ARG-575;
RP PRO-2023; ALA-2109 AND ALA-2339.
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 [6]
RP VARIANT [LARGE SCALE ANALYSIS] MET-484.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Plays a role of transcription factor; binds to recognition
CC signal sequences (Rss heptamer) for somatic recombination of
CC immunoglobulin and T-cell receptor gene segments; Binds also to the
CC kappa-B motif of gene such as S100A4, involved in cell progression and
CC differentiation. Kappa-B motif is a gene regulatory element found in
CC promoters and enhancers of genes involved in immunity, inflammation,
CC and growth and that responds to viral antigens, mitogens, and
CC cytokines. Involvement of HIVEP3 in cell growth is strengthened by the
CC fact that its down-regulation promotes cell cycle progression with
CC ultimate formation of multinucleated giant cells. Strongly inhibits
CC TNF-alpha-induced NF-kappa-B activation; Interferes with nuclear factor
CC NF-kappa-B by several mechanisms: as transcription factor, by competing
CC for Kappa-B motif and by repressing transcription in the nucleus;
CC through a non transcriptional process, by inhibiting nuclear
CC translocation of RELA by association with TRAF2, an adapter molecule in
CC the tumor necrosis factor signaling, which blocks the formation of IKK
CC complex. Interaction with TRAF proteins inhibits both NF-Kappa-B-
CC mediated and c-Jun N-terminal kinase/JNK-mediated responses that
CC include apoptosis and pro-inflammatory cytokine gene expression.
CC Positively regulates the expression of IL2 in T-cell. Essential
CC regulator of adult bone formation. {ECO:0000269|PubMed:11161801}.
CC -!- SUBUNIT: Interacts with TRAF1 AND TRAF2 as well as with JUN. Forms a
CC multimeric complex with RUNX2 and E3 ubiquitin ligase WWP1 (By
CC similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q5T1R4; P31947: SFN; NbExp=5; IntAct=EBI-28989979, EBI-476295;
CC Q5T1R4; P61981: YWHAG; NbExp=2; IntAct=EBI-28989979, EBI-359832;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms can be generated by alternative splicing
CC or polyadenylation. HIVEP3L transcript may lack exon 7 leading to a
CC premature codon stop. {ECO:0000269|PubMed:11161801};
CC Name=1; Synonyms=HIVEP3S;
CC IsoId=Q5T1R4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5T1R4-2; Sequence=VSP_033279;
CC -!- INDUCTION: By 12-O-tetradecanoylphorbol-13 acetate (TPA).
CC -!- DOMAIN: The ZAS2 domain binds DNA as dimers, tetramers, and multiple of
CC tetramers and readily forms highly ordered DNA-protein structures.
CC {ECO:0000250}.
CC -!- PTM: Phosphorylated on threonine and serine residues. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB13381.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF278765; AAK01082.1; -; mRNA.
DR EMBL; AB046775; BAB13381.2; ALT_INIT; mRNA.
DR EMBL; AL445933; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC152563; AAI52564.1; -; mRNA.
DR CCDS; CCDS44124.1; -. [Q5T1R4-2]
DR CCDS; CCDS463.1; -. [Q5T1R4-1]
DR RefSeq; NP_001121186.1; NM_001127714.2. [Q5T1R4-2]
DR RefSeq; NP_078779.2; NM_024503.4. [Q5T1R4-1]
DR RefSeq; XP_011540186.1; XM_011541884.2. [Q5T1R4-1]
DR RefSeq; XP_016857481.1; XM_017001992.1. [Q5T1R4-1]
DR RefSeq; XP_016857482.1; XM_017001993.1. [Q5T1R4-1]
DR RefSeq; XP_016857483.1; XM_017001994.1. [Q5T1R4-2]
DR AlphaFoldDB; Q5T1R4; -.
DR SMR; Q5T1R4; -.
DR BioGRID; 121861; 14.
DR CORUM; Q5T1R4; -.
DR IntAct; Q5T1R4; 9.
DR MINT; Q5T1R4; -.
DR STRING; 9606.ENSP00000361664; -.
DR GlyGen; Q5T1R4; 7 sites, 1 O-linked glycan (7 sites).
DR iPTMnet; Q5T1R4; -.
DR PhosphoSitePlus; Q5T1R4; -.
DR BioMuta; HIVEP3; -.
DR DMDM; 74756245; -.
DR EPD; Q5T1R4; -.
DR jPOST; Q5T1R4; -.
DR MassIVE; Q5T1R4; -.
DR MaxQB; Q5T1R4; -.
DR PaxDb; Q5T1R4; -.
DR PeptideAtlas; Q5T1R4; -.
DR PRIDE; Q5T1R4; -.
DR ProteomicsDB; 64282; -. [Q5T1R4-1]
DR ProteomicsDB; 64283; -. [Q5T1R4-2]
DR Antibodypedia; 32189; 28 antibodies from 8 providers.
DR DNASU; 59269; -.
DR Ensembl; ENST00000372583.6; ENSP00000361664.1; ENSG00000127124.16. [Q5T1R4-1]
DR Ensembl; ENST00000372584.5; ENSP00000361665.1; ENSG00000127124.16. [Q5T1R4-2]
DR Ensembl; ENST00000643665.1; ENSP00000494598.1; ENSG00000127124.16. [Q5T1R4-2]
DR GeneID; 59269; -.
DR KEGG; hsa:59269; -.
DR MANE-Select; ENST00000372583.6; ENSP00000361664.1; NM_024503.5; NP_078779.2.
DR UCSC; uc001cgz.5; human. [Q5T1R4-1]
DR CTD; 59269; -.
DR DisGeNET; 59269; -.
DR GeneCards; HIVEP3; -.
DR HGNC; HGNC:13561; HIVEP3.
DR HPA; ENSG00000127124; Tissue enhanced (lymphoid).
DR MIM; 606649; gene.
DR neXtProt; NX_Q5T1R4; -.
DR OpenTargets; ENSG00000127124; -.
DR PharmGKB; PA29299; -.
DR VEuPathDB; HostDB:ENSG00000127124; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000157218; -.
DR HOGENOM; CLU_000719_1_0_1; -.
DR InParanoid; Q5T1R4; -.
DR OMA; QEKTGQP; -.
DR OrthoDB; 212048at2759; -.
DR PhylomeDB; Q5T1R4; -.
DR TreeFam; TF331837; -.
DR PathwayCommons; Q5T1R4; -.
DR Reactome; R-HSA-8939902; Regulation of RUNX2 expression and activity.
DR SignaLink; Q5T1R4; -.
DR BioGRID-ORCS; 59269; 22 hits in 1093 CRISPR screens.
DR ChiTaRS; HIVEP3; human.
DR GeneWiki; HIVEP3; -.
DR GenomeRNAi; 59269; -.
DR Pharos; Q5T1R4; Tbio.
DR PRO; PR:Q5T1R4; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q5T1R4; protein.
DR Bgee; ENSG00000127124; Expressed in buccal mucosa cell and 153 other tissues.
DR Genevisible; Q5T1R4; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0035914; P:skeletal muscle cell differentiation; IEA:Ensembl.
DR InterPro; IPR034729; ZF_CCHC_HIVEP.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 4.
DR SMART; SM00355; ZnF_C2H2; 5.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS51811; ZF_CCHC_HIVEP; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..2406
FT /note="Transcription factor HIVEP3"
FT /id="PRO_0000331627"
FT REPEAT 1964..1967
FT /note="1"
FT REPEAT 1970..1973
FT /note="2"
FT REPEAT 1993..1996
FT /note="3"
FT REPEAT 1998..2001
FT /note="4"
FT REPEAT 2067..2070
FT /note="5"
FT REPEAT 2079..2082
FT /note="6"
FT ZN_FING 192..214
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 220..242
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 640..670
FT /note="CCHC HIVEP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01154"
FT ZN_FING 1754..1776
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1782..1806
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 192..242
FT /note="ZAS1"
FT REGION 211..1074
FT /note="No DNA binding activity or transactivation activity,
FT but complete prevention of TRAF-dependent NF-Kappa-B
FT activation; associates with TRAF2 and JUN"
FT /evidence="ECO:0000250"
FT REGION 264..287
FT /note="Acidic 1"
FT REGION 272..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 481..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 597..633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 677..696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 706..1115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 862..883
FT /note="Acidic 2"
FT REGION 1268..1303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1406..1459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1472..1594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1692..1727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1754..1806
FT /note="ZAS2"
FT REGION 1817..1872
FT /note="Acidic 3"
FT REGION 1818..2033
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2052..2113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2053..2148
FT /note="6 X 4 AA tandem repeats of S-P-X-[RK]"
FT REGION 2125..2151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2224..2406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1442..1466
FT /evidence="ECO:0000255"
FT MOTIF 903..909
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 1..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..336
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..409
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 615..633
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 709..730
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 797..812
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 861..884
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 914..946
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 992..1019
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1069..1094
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1268..1283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1406..1430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1445..1459
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1476..1490
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1494..1508
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1569..1594
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1700..1724
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1829..1848
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1849..1873
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1910..1937
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1986..2002
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2129..2149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2244..2262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2304..2318
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 2136
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10997877,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_033279"
FT VARIANT 35
FT /note="V -> I (in dbSNP:rs2146315)"
FT /id="VAR_042910"
FT VARIANT 484
FT /note="V -> M (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs780211835)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_042911"
FT VARIANT 575
FT /note="H -> R (in dbSNP:rs2810566)"
FT /evidence="ECO:0000269|PubMed:10997877,
FT ECO:0000269|PubMed:11161801, ECO:0000269|PubMed:15489334"
FT /id="VAR_042912"
FT VARIANT 1087
FT /note="Q -> H (in dbSNP:rs17363472)"
FT /id="VAR_042913"
FT VARIANT 2023
FT /note="A -> P (in dbSNP:rs2483689)"
FT /evidence="ECO:0000269|PubMed:10997877,
FT ECO:0000269|PubMed:11161801, ECO:0000269|PubMed:15489334"
FT /id="VAR_042914"
FT VARIANT 2109
FT /note="D -> A (in dbSNP:rs2991344)"
FT /evidence="ECO:0000269|PubMed:10997877,
FT ECO:0000269|PubMed:11161801, ECO:0000269|PubMed:15489334"
FT /id="VAR_042915"
FT VARIANT 2272
FT /note="G -> R (in dbSNP:rs11809423)"
FT /evidence="ECO:0000269|PubMed:11161801"
FT /id="VAR_042916"
FT VARIANT 2339
FT /note="T -> A (in dbSNP:rs9439043)"
FT /evidence="ECO:0000269|PubMed:10997877,
FT ECO:0000269|PubMed:11161801, ECO:0000269|PubMed:15489334"
FT /id="VAR_042917"
FT CONFLICT 44
FT /note="A -> P (in Ref. 1; AAK01082)"
FT /evidence="ECO:0000305"
FT CONFLICT 94..95
FT /note="QL -> HV (in Ref. 1; AAK01082)"
FT /evidence="ECO:0000305"
FT CONFLICT 123
FT /note="D -> S (in Ref. 1; AAK01082)"
FT /evidence="ECO:0000305"
FT CONFLICT 127
FT /note="P -> L (in Ref. 1; AAK01082)"
FT /evidence="ECO:0000305"
FT CONFLICT 133..134
FT /note="FV -> LL (in Ref. 1; AAK01082)"
FT /evidence="ECO:0000305"
FT CONFLICT 589
FT /note="R -> P (in Ref. 1; AAK01082)"
FT /evidence="ECO:0000305"
FT CONFLICT 901
FT /note="L -> A (in Ref. 1; AAK01082)"
FT /evidence="ECO:0000305"
FT CONFLICT 961
FT /note="S -> D (in Ref. 1; AAK01082)"
FT /evidence="ECO:0000305"
FT CONFLICT 1034..1035
FT /note="RV -> GE (in Ref. 1; AAK01082)"
FT /evidence="ECO:0000305"
FT CONFLICT 1048..1049
FT /note="QA -> SP (in Ref. 1; AAK01082)"
FT /evidence="ECO:0000305"
FT CONFLICT 1110
FT /note="P -> A (in Ref. 1; AAK01082)"
FT /evidence="ECO:0000305"
FT CONFLICT 1180
FT /note="P -> L (in Ref. 2; BAB13381 and 5; AAI52564)"
FT /evidence="ECO:0000305"
FT CONFLICT 1279
FT /note="T -> Q (in Ref. 1; AAK01082)"
FT /evidence="ECO:0000305"
FT CONFLICT 1524
FT /note="T -> Q (in Ref. 1; AAK01082)"
FT /evidence="ECO:0000305"
FT CONFLICT 2376
FT /note="P -> S (in Ref. 1; AAK01082)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2406 AA; 259465 MW; AFCCFDAF87014A7D CRC64;
MDPEQSVKGT KKAEGSPRKR LTKGEAIQTS VSSSVPYPGS GTAATQESPA QELLAPQPFP
GPSSVLREGS QEKTGQQQKP PKRPPIEASV HISQLPQHPL TPAFMSPGKP EHLLEGSTWQ
LVDPMRPGPS GSFVAPGLHP QSQLLPSHAS IIPPEDLPGV PKVFVPRPSQ VSLKPTEEAH
KKERKPQKPG KYICQYCSRP CAKPSVLQKH IRSHTGERPY PCGPCGFSFK TKSNLYKHRK
SHAHRIKAGL ASGMGGEMYP HGLEMERIPG EEFEEPTEGE STDSEEETSA TSGHPAELSP
RPKQPLLSSG LYSSGSHSSS HERCSLSQSS TAQSLEDPPP FVEPSSEHPL SHKPEDTHTI
KQKLALRLSE RKKVIDEQAF LSPGSKGSTE SGYFSRSESA EQQVSPPNTN AKSYAEIIFG
KCGRIGQRTA MLTATSTQPL LPLSTEDKPS LVPLSVPRTQ VIEHITKLIT INEAVVDTSE
IDSVKPRRSS LSRRSSMESP KSSLYREPLS SHSEKTKPEQ SLLSLQHPPS TAPPVPLLRS
HSMPSAACTI STPHHPFRGS YSFDDHITDS EALSHSSHVF TSHPRMLKRQ PAIELPLGGE
YSSEEPGPSS KDTASKPSDE VEPKESELTK KTKKGLKTKG VIYECNICGA RYKKRDNYEA
HKKYYCSELQ IAKPISAGTH TSPEAEKSQI EHEPWSQMMH YKLGTTLELT PLRKRRKEKS
LGDEEEPPAF ESTKSQFGSP GPSDAARNLP LESTKSPAEP SKSVPSLEGP TGFQPRTPKP
GSGSESGKER RTTSKEISVI QHTSSFEKSD SLEQPSGLEG EDKPLAQFPS PPPAPHGRSA
HSLQPKLVRQ PNIQVPEILV TEEPDRPDTE PEPPPKEPEK TEEFQWPQRS QTLAQLPAEK
LPPKKKRLRL AEMAQSSGES SFESSVPLSR SPSQESNVSL SGSSRSASFE RDDHGKAEAP
SPSSDMRPKP LGTHMLTVPS HHPHAREMRR SASEQSPNVS HSAHMTETRS KSFDYGSLSL
TGPSAPAPVA PPARVAPPER RKCFLVRQAS LSRPPESELE VAPKGRQESE EPQPSSSKPS
AKSSLSQISS AATSHGGPPG GKGPGQDRPP LGPTVPYTEA LQVFHHPVAQ TPLHEKPYLP
PPVSLFSFQH LVQHEPGQSP EFFSTQAMSS LLSSPYSMPP LPPSLFQAPP LPLQPTVLHP
GQLHLPQLMP HPANIPFRQP PSFLPMPYPT SSALSSGFFL PLQSQFALQL PGDVESHLPQ
IKTSLAPLAT GSAGLSPSTE YSSDIRLPPV APPASSSAPT SAPPLALPAC PDTMVSLVVP
VRVQTNMPSY GSAMYTTLSQ ILVTQSQGSS ATVALPKFEE PPSKGTTVCG ADVHEVGPGP
SGLSEEQSRA FPTPYLRVPV TLPERKGTSL SSESILSLEG SSSTAGGSKR VLSPAGSLEL
TMETQQQKRV KEEEASKADE KLELVKPCSV VLTSTEDGKR PEKSHLGNQG QGRRELEMLS
SLSSDPSDTK EIPPLPHPAL SHGTAPGSEA LKEYPQPSGK PHRRGLTPLS VKKEDSKEQP
DLPSLAPPSS LPLSETSSRP AKSQEGTDSK KVLQFPSLHT TTNVSWCYLN YIKPNHIQHA
DRRSSVYAGW CISLYNPNLP GVSTKAALSL LRSKQKVSKE TYTMATAPHP EAGRLVPSSS
RKPRMTEVHL PSLVSPEGQK DLARVEKEEE RRGEPEEDAP ASQRGEPARI KIFEGGYKSN
EEYVYVRGRG RGKYVCEECG IRCKKPSMLK KHIRTHTDVR PYVCKHCHFA FKTKGNLTKH
MKSKAHSKKC QETGVLEELE AEEGTSDDLF QDSEGREGSE AVEEHQFSDL EDSDSDSDLD
EDEDEDEEES QDELSRPSSE APPPGPPHAL RADSSPILGP QPPDAPASGT EATRGSSVSE
AERLTASSCS MSSQSMPGLP WLGPAPLGSV EKDTGSALSY KPVSPRRPWS PSKEAGSRPP
LARKHSLTKN DSSPQRCSPA REPQASAPSP PGLHVDPGRG MGALPCGSPR LQLSPLTLCP
LGRELAPRAH VLSKLEGTTD PGLPRYSPTR RWSPGQAESP PRSAPPGKWA LAGPGSPSAG
EHGPGLGLDP RVLFPPAPLP HKLLSRSPET CASPWQKAES RSPSCSPGPA HPLSSRPFSA
LHDFHGHILA RTEENIFSHL PLHSQHLTRA PCPLIPIGGI QMVQARPGAH PTLLPGPTAA
WVSGFSGGGS DLTGAREAQE RGRWSPTESS SASVSPVAKV SKFTLSSELE GGDYPKERER
TGGGPGRPPD WTPHGTGAPA EPTPTHSPCT PPDTLPRPPQ GRRAAQSWSP RLESPRAPTN
PEPSATPPLD RSSSVGCLAE ASARFPARTR NLSGEPRTRQ DSPKPSGSGE PRAHPHQPED
RVPPNA
