KDM5C_MOUSE
ID KDM5C_MOUSE Reviewed; 1554 AA.
AC P41230; O54995; Q3TYU8; Q3U1X6; Q3U282; Q6ZQF8; Q80XQ9; Q9CVI4; Q9D0C3;
AC Q9QVR8; Q9R039;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 4.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Lysine-specific demethylase 5C;
DE EC=1.14.11.67 {ECO:0000250|UniProtKB:P41229};
DE AltName: Full=Histone demethylase JARID1C;
DE AltName: Full=Jumonji/ARID domain-containing protein 1C;
DE AltName: Full=Protein SmcX;
DE AltName: Full=Protein Xe169;
DE AltName: Full=[histone H3]-trimethyl-L-lysine(4) demethylase 5C {ECO:0000305};
GN Name=Kdm5c; Synonyms=Jarid1c, Kiaa0234, Smcx, Xe169;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=129/SvJ;
RX PubMed=10441747; DOI=10.1007/s003359901116;
RA Agulnik A.I., Longepied G., Ty M.T., Bishop C.E., Mitchell M.J.;
RT "Mouse H-Y encoding Smcy gene and its X chromosomal homolog Smcx.";
RL Mamm. Genome 10:926-929(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Dendritic cell, Embryo, Inner ear, and Small intestine;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 36-1068.
RC STRAIN=BALB/cJ; TISSUE=Testis;
RX PubMed=7951230; DOI=10.1093/hmg/3.6.879;
RA Agulnik A.I., Mitchell M.J., Mattei M.-G., Borsani G., Avner P.A.,
RA Lerner J.L., Bishop C.E.;
RT "A novel X gene with a widely transcribed Y-linked homologue escapes X-
RT inactivation in mouse and human.";
RL Hum. Mol. Genet. 3:879-884(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 165-1554 (ISOFORM 1).
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1206-1385 (ISOFORM 1).
RX PubMed=7951318; DOI=10.1038/ng0894-491;
RA Wu J., Salido E., Yen P., Mohandas T., Shapiro L.J.;
RT "The murine Xe169 gene escapes X-inactivation like its human homologue.";
RL Nat. Genet. 7:491-496(1994).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-39.
RX PubMed=9723615; DOI=10.1038/29522;
RA Jegalian K.G., Page D.C.;
RT "A proposed path by which genes common to mammalian X and Y chromosomes
RT evolve to become X inactivated.";
RL Nature 394:776-780(1998).
RN [8]
RP FUNCTION.
RC STRAIN=C3H/HeJ;
RX PubMed=7544442; DOI=10.1038/376695a0;
RA Scott D.M., Ehrmann I.E., Ellis P.S., Bishop C.E., Agulnik A.I.,
RA Simpson E., Mitchell M.J.;
RT "Identification of a mouse male-specific transplantation antigen, H-Y.";
RL Nature 376:695-698(1995).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-317 AND SER-893, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP FUNCTION.
RX PubMed=21960634; DOI=10.1126/science.1206022;
RA DiTacchio L., Le H.D., Vollmers C., Hatori M., Witcher M., Secombe J.,
RA Panda S.;
RT "Histone lysine demethylase JARID1a activates CLOCK-BMAL1 and influences
RT the circadian clock.";
RL Science 333:1881-1885(2011).
CC -!- FUNCTION: Histone demethylase that specifically demethylates 'Lys-4' of
CC histone H3, thereby playing a central role in histone code. Does not
CC demethylate histone H3 'Lys-9', H3 'Lys-27', H3 'Lys-36', H3 'Lys-79'
CC or H4 'Lys-20'. Demethylates trimethylated and dimethylated but not
CC monomethylated H3 'Lys-4'. Participates in transcriptional repression
CC of neuronal genes by recruiting histone deacetylases and REST at
CC neuron-restrictive silencer elements (By similarity). Represses the
CC CLOCK-ARNTL/BMAL1 heterodimer-mediated transcriptional activation of
CC the core clock component PER2. {ECO:0000250|UniProtKB:P41229,
CC ECO:0000269|PubMed:21960634}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(4)-
CC [histone H3] + 3 O2 = 3 CO2 + 3 formaldehyde + L-lysyl(4)-[histone
CC H3] + 3 succinate; Xref=Rhea:RHEA:60208, Rhea:RHEA-COMP:15537,
CC Rhea:RHEA-COMP:15547, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:61961; EC=1.14.11.67;
CC Evidence={ECO:0000250|UniProtKB:P41229};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:P41229};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250|UniProtKB:P41229};
CC -!- SUBUNIT: Part of two distinct complexes, one containing E2F6, and the
CC other containing REST. {ECO:0000250|UniProtKB:P41229}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00355,
CC ECO:0000255|PROSITE-ProRule:PRU00537}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P41230-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P41230-2; Sequence=VSP_000316;
CC Name=3;
CC IsoId=P41230-3; Sequence=VSP_026411, VSP_000316;
CC -!- DOMAIN: The first PHD-type zinc finger domain recognizes and binds H3-
CC K9Me3. {ECO:0000250}.
CC -!- DOMAIN: Both the JmjC domain and the JmjN domain are required for
CC enzymatic activity. {ECO:0000250}.
CC -!- MISCELLANEOUS: Escapes X-inactivation.
CC -!- SIMILARITY: Belongs to the JARID1 histone demethylase family.
CC {ECO:0000305}.
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DR EMBL; AF127245; AAD53049.1; -; mRNA.
DR EMBL; AK008105; BAB25462.1; -; mRNA.
DR EMBL; AK155279; BAE33161.1; -; mRNA.
DR EMBL; AK155427; BAE33260.1; -; mRNA.
DR EMBL; AK155651; BAE33367.1; -; mRNA.
DR EMBL; AK158340; BAE34464.1; -; mRNA.
DR EMBL; AK011577; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC043096; AAH43096.1; -; mRNA.
DR EMBL; BC054550; AAH54550.1; -; mRNA.
DR EMBL; Z29651; CAA82759.1; -; mRNA.
DR EMBL; AK129096; BAC97906.1; -; mRNA.
DR EMBL; L29563; AAA62384.1; -; mRNA.
DR EMBL; AF039894; AAB96762.1; -; mRNA.
DR CCDS; CCDS41178.1; -. [P41230-2]
DR PIR; I48775; I48775.
DR PIR; I84689; I84689.
DR RefSeq; NP_038696.2; NM_013668.4. [P41230-2]
DR RefSeq; XP_006528832.1; XM_006528769.3. [P41230-1]
DR RefSeq; XP_006528835.1; XM_006528772.3. [P41230-3]
DR AlphaFoldDB; P41230; -.
DR BMRB; P41230; -.
DR SMR; P41230; -.
DR BioGRID; 203341; 5.
DR IntAct; P41230; 2.
DR MINT; P41230; -.
DR STRING; 10090.ENSMUSP00000108203; -.
DR iPTMnet; P41230; -.
DR PhosphoSitePlus; P41230; -.
DR EPD; P41230; -.
DR jPOST; P41230; -.
DR MaxQB; P41230; -.
DR PaxDb; P41230; -.
DR PeptideAtlas; P41230; -.
DR PRIDE; P41230; -.
DR ProteomicsDB; 269290; -. [P41230-1]
DR ProteomicsDB; 269291; -. [P41230-2]
DR ProteomicsDB; 269292; -. [P41230-3]
DR Antibodypedia; 26540; 218 antibodies from 31 providers.
DR DNASU; 20591; -.
DR Ensembl; ENSMUST00000082177; ENSMUSP00000080814; ENSMUSG00000025332. [P41230-3]
DR Ensembl; ENSMUST00000112584; ENSMUSP00000108203; ENSMUSG00000025332. [P41230-1]
DR Ensembl; ENSMUST00000112588; ENSMUSP00000108207; ENSMUSG00000025332. [P41230-2]
DR GeneID; 20591; -.
DR KEGG; mmu:20591; -.
DR UCSC; uc009uqc.3; mouse. [P41230-2]
DR UCSC; uc009uqd.3; mouse. [P41230-3]
DR UCSC; uc009uqe.3; mouse. [P41230-1]
DR CTD; 8242; -.
DR MGI; MGI:99781; Kdm5c.
DR VEuPathDB; HostDB:ENSMUSG00000025332; -.
DR eggNOG; KOG1246; Eukaryota.
DR GeneTree; ENSGT00940000161236; -.
DR HOGENOM; CLU_000991_2_2_1; -.
DR InParanoid; P41230; -.
DR OMA; ASAHSWK; -.
DR OrthoDB; 664180at2759; -.
DR PhylomeDB; P41230; -.
DR TreeFam; TF106476; -.
DR Reactome; R-MMU-3214842; HDMs demethylate histones.
DR BioGRID-ORCS; 20591; 11 hits in 79 CRISPR screens.
DR ChiTaRS; Kdm5c; mouse.
DR PRO; PR:P41230; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; P41230; protein.
DR Bgee; ENSMUSG00000025332; Expressed in epithelium of lens and 235 other tissues.
DR ExpressionAtlas; P41230; baseline and differential.
DR Genevisible; P41230; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0032452; F:histone demethylase activity; IBA:GO_Central.
DR GO; GO:0032453; F:histone H3-methyl-lysine-4 demethylase activity; ISO:MGI.
DR GO; GO:0034647; F:histone H3-tri/di/monomethyl-lysine-4 demethylase activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; ISO:MGI.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0034720; P:histone H3-K4 demethylation; IDA:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0042752; P:regulation of circadian rhythm; NAS:UniProtKB.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR Gene3D; 1.10.150.60; -; 1.
DR Gene3D; 3.30.40.10; -; 2.
DR InterPro; IPR001606; ARID_dom.
DR InterPro; IPR036431; ARID_dom_sf.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR003349; JmjN.
DR InterPro; IPR013637; Lys_sp_deMease-like_dom.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR004198; Znf_C5HC2.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF01388; ARID; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF02375; JmjN; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF08429; PLU-1; 1.
DR Pfam; PF02928; zf-C5HC2; 1.
DR SMART; SM00501; BRIGHT; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00545; JmjN; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF46774; SSF46774; 1.
DR SUPFAM; SSF57903; SSF57903; 2.
DR PROSITE; PS51011; ARID; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS51183; JMJN; 1.
DR PROSITE; PS01359; ZF_PHD_1; 2.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Biological rhythms; Chromatin regulator; Dioxygenase;
KW Iron; Isopeptide bond; Metal-binding; Nucleus; Oxidoreductase;
KW Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..1554
FT /note="Lysine-specific demethylase 5C"
FT /id="PRO_0000200587"
FT DOMAIN 14..55
FT /note="JmjN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00537"
FT DOMAIN 79..169
FT /note="ARID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00355"
FT DOMAIN 468..634
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT ZN_FING 326..372
FT /note="PHD-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 1187..1248
FT /note="PHD-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 197..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 284..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1319..1364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1437..1535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..227
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..303
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1455..1483
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 514
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 517
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 602
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT MOD_RES 287
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P41229"
FT MOD_RES 301
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P41229"
FT MOD_RES 317
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 893
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 897
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P41229"
FT MOD_RES 1353
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P41229"
FT CROSSLNK 205
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P41229"
FT CROSSLNK 229
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P41229"
FT CROSSLNK 244
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P41229"
FT CROSSLNK 274
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P41229"
FT CROSSLNK 295
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P41229"
FT CROSSLNK 1127
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P41229"
FT VAR_SEQ 77..117
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_026411"
FT VAR_SEQ 1364..1366
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:10441747,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072"
FT /id="VSP_000316"
FT CONFLICT 3
FT /note="L -> M (in Ref. 7; AAB96762)"
FT /evidence="ECO:0000305"
FT CONFLICT 26
FT /note="D -> G (in Ref. 7; AAB96762)"
FT /evidence="ECO:0000305"
FT CONFLICT 123
FT /note="G -> S (in Ref. 2; BAE33161/BAE33260)"
FT /evidence="ECO:0000305"
FT CONFLICT 249
FT /note="G -> D (in Ref. 2; BAE34464)"
FT /evidence="ECO:0000305"
FT CONFLICT 726
FT /note="D -> N (in Ref. 5; BAC97906)"
FT /evidence="ECO:0000305"
FT CONFLICT 865
FT /note="C -> L (in Ref. 1; AAD53049 and 4; CAA82759)"
FT /evidence="ECO:0000305"
FT CONFLICT 1068
FT /note="L -> P (in Ref. 4; CAA82759)"
FT /evidence="ECO:0000305"
FT CONFLICT 1126
FT /note="Y -> C (in Ref. 2; BAE33367)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1554 AA; 175313 MW; 585EA9F890B0D9A0 CRC64;
MELGSDDFLP PPECPVFEPS WAEFRDPLGY IAKIRPIAEK SGICKIRPPA DWQPPFAVEV
DNFRFTPRIQ RLNELEAQTR VKLNYLDQIA KFWEIQGSSL KIPNVERRIL DLYSLSKIVV
EEGGYETICK DRRWARVAQR LNYPPGKNIG SLLRSHYERI VYPYEMYQSG ANLVQCNTRP
FDNEEKDKEY KPHSIPLRQS VQPSKFNSYG RRAKRLQPDP EPTEEDIEKN PELKKLQIYG
AGPKMMGLGL MAKDKTLRKK DKEGPECPPT VVVKEELGGD VKMESTSPKT FLEGKEELSH
SPEPCTKMTM RLRRNHSNAQ FIESYVCRMC SRGDEDDKLL LCDGCDDNYH IFCLLPPLPE
IPKGVWRCPK CVMAECKRPP EAFGFEQATR EYTLQSFGEM ADSFKADYFN MPVHMVPTEL
VEKEFWRLVN SIEEDVTVEY GADIHSKEFG SGFPVSDSKR HLTPEEEEYA TSGWNLNVMP
VLEQSVLCHI NADISGMKVP WLYVGMVFSA FCWHIEDHWS YSINYLHWGE PKTWYGVPSL
AAEHLEEVMK KLTPELFDSQ PDLLHQLVTL MNPNTLMSHG VPVVRTNQCA GEFVITFPRA
YHSGFNQGYN FAEAVNFCTA DWLPAGRQCI EHYRRLRRYC VFSHEELICK MAACPEKLDL
NLAAAVHKEM FIMVQEERRL RKALLEKGIT EAEREAFELL PDDERQCIKC KTTCFLSALA
CYDCPDGLVC LSHINDLCKC SSSRQYLRYR YTLDELPAML HKLKVRAESF DTWANKVRVA
LEVEDGRKRS LEELRALESE ARERRFPNSE LLQRLKNCLS EAEACVSRAL GLVSGQEAGP
DRVAGLQMTL AELRDFLGQM NNLPCAMHQI GDVKGILEQV EAYQTEAREA LVSQPSSPGL
LQSLLERGQQ LGVEVPEAQQ LQRQVEQARW LDEVKRTLAP SARRGTLAIM RGLLVAGASV
APSPAVDKAQ AELQELLTIA ERWEEKAHLC LEARQKHPPA TLEAIIHEAE NIPVHLPNIQ
SLKEALAKAR AWIADVDEIQ NGDHYPCLDD LEGLVAVGRD LPVGLEELRQ LELQVLTAHS
WREKASKTFL KKNSCYTLLE VLCPCADAGS DSTKRSRWME KELGLYKSDT ELLGLSAQDL
RDPGSVIVAF KEGEQKEKEG ILQLRRTNSA KPSPLALLTT ASSTASICVC GQVPAGVGAL
QCDLCQDWFH GRCVTVPRLL SSQRSSLPSS PLLAWWEWDT KFLCPLCMRS RRPRLETILA
LLVALQRLPV RLPEGEALQC LTERAISWQG RARQVLASEE VTALLGRLAE LRQRLQAESK
PEESLAYPSD GGEGTGNMPK VQGLLENGDS VTSPEKVATE EGSGKRDLEL LSSILPQLSG
PVLELPEATR APLEELMMEG DLLEVTLDEN HSIWQLLQAG QPPDLKRVQT LLELEKAERH
GSRTRGRALE RRRRRKVDRG GEPDDPAREE LEPKRVRSSG PEAEEVQEEE ELEEETGGEV
PPVPFPNSGS PSIQEDQDGL EPVLEAGSDT SAPFSTLTSR LLMSCPQQPS LQQL
