ZNF74_HUMAN
ID ZNF74_HUMAN Reviewed; 644 AA.
AC Q16587; B5MCE3; B7Z5Y2; Q6IBV2; Q6PJP1; Q9UC04; Q9UF05; Q9UF06; Q9UF07;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 3.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Zinc finger protein 74;
DE AltName: Full=Zinc finger protein 520;
DE AltName: Full=hZNF7;
GN Name=ZNF74; Synonyms=ZNF520;
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).
RC TISSUE=Brain;
RX PubMed=8663113; DOI=10.1074/jbc.271.26.15458;
RA Grondin B., Bazinet M., Aubry M.;
RT "The KRAB zinc finger gene ZNF74 encodes an RNA-binding protein tightly
RT associated with the nuclear matrix.";
RL J. Biol. Chem. 271:15458-15467(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=8268910; DOI=10.1093/hmg/2.10.1583;
RA Aubry M., Demczuk S., Desmaze C., Aikem M., Aurias M., Julien J.-P.,
RA Rouleau G.A.;
RT "Isolation of a zinc finger gene consistently deleted in DiGeorge
RT syndrome.";
RL Hum. Mol. Genet. 2:1583-1587(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RA Aubry M., Cote F.;
RT "Alternative promoter usage and splicing of ZNF74 gene.";
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT LYS-117.
RC TISSUE=Brain;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 5).
RC TISSUE=Muscle, and Retinoblastoma;
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 [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 499-583.
RX PubMed=1639391; DOI=10.1016/0888-7543(92)90135-f;
RA Aubry M., Marineau C., Zhang F.R., Zahed L., Figlewicz D., Delattre O.,
RA Thomas G., de Jong P.J., Julien J.-P., Rouleau G.A.;
RT "Cloning of six new genes with zinc finger motifs mapping to short and long
RT arms of human acrocentric chromosome 22 (p and q11.2).";
RL Genomics 13:641-648(1992).
RN [9]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-582, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [10]
RP VARIANTS LYS-117 AND 623-ASN-PHE-624.
RX PubMed=11705709; DOI=10.1016/s0920-9964(00)00191-2;
RA Takase K., Ohtsuki T., Migita O., Toru M., Inada T., Yamakawa-Kobayashi K.,
RA Arinami T.;
RT "Association of ZNF74 gene genotypes with age-at-onset of schizophrenia.";
RL Schizophr. Res. 52:161-165(2001).
CC -!- FUNCTION: May play a role in RNA metabolism.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=2;
CC IsoId=Q16587-1; Sequence=Displayed;
CC Name=1;
CC IsoId=Q16587-2; Sequence=VSP_006891;
CC Name=3;
CC IsoId=Q16587-3; Sequence=VSP_006892;
CC Name=4;
CC IsoId=Q16587-4; Sequence=VSP_006893;
CC Name=5;
CC IsoId=Q16587-5; Sequence=VSP_045530, VSP_045531;
CC -!- TISSUE SPECIFICITY: Highly expressed in the fetal brain.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF21777.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAF21778.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAF21779.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAF21780.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA50632.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA63379.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X92715; CAA63379.1; ALT_FRAME; mRNA.
DR EMBL; X71623; CAA50632.1; ALT_FRAME; mRNA.
DR EMBL; CR456616; CAG30502.1; -; mRNA.
DR EMBL; AF072567; AAF21777.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AF072557; AAF21777.1; JOINED; Genomic_DNA.
DR EMBL; AF072562; AAF21777.1; JOINED; Genomic_DNA.
DR EMBL; AF072567; AAF21778.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AF072557; AAF21778.1; JOINED; Genomic_DNA.
DR EMBL; AF072562; AAF21778.1; JOINED; Genomic_DNA.
DR EMBL; AF072567; AAF21779.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AF072562; AAF21779.1; JOINED; Genomic_DNA.
DR EMBL; AF072567; AAF21780.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AF072562; AAF21780.1; JOINED; Genomic_DNA.
DR EMBL; AK299569; BAH13068.1; -; mRNA.
DR EMBL; AC007731; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC013395; AAH13395.1; -; mRNA.
DR EMBL; BC056902; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; X63182; CAC16149.1; -; Genomic_DNA.
DR CCDS; CCDS42982.1; -. [Q16587-1]
DR CCDS; CCDS58794.1; -. [Q16587-5]
DR PIR; I39311; I39311.
DR RefSeq; NP_001243452.1; NM_001256523.1. [Q16587-5]
DR RefSeq; NP_001243453.1; NM_001256524.1. [Q16587-1]
DR RefSeq; NP_001243454.1; NM_001256525.1. [Q16587-2]
DR RefSeq; NP_003417.2; NM_003426.3. [Q16587-1]
DR AlphaFoldDB; Q16587; -.
DR SMR; Q16587; -.
DR BioGRID; 113444; 35.
DR IntAct; Q16587; 4.
DR MINT; Q16587; -.
DR STRING; 9606.ENSP00000483077; -.
DR iPTMnet; Q16587; -.
DR PhosphoSitePlus; Q16587; -.
DR BioMuta; ZNF74; -.
DR DMDM; 292495055; -.
DR EPD; Q16587; -.
DR jPOST; Q16587; -.
DR MassIVE; Q16587; -.
DR PaxDb; Q16587; -.
DR PeptideAtlas; Q16587; -.
DR PRIDE; Q16587; -.
DR ProteomicsDB; 6037; -.
DR ProteomicsDB; 60933; -. [Q16587-1]
DR ProteomicsDB; 60934; -. [Q16587-2]
DR ProteomicsDB; 60935; -. [Q16587-3]
DR ProteomicsDB; 60936; -. [Q16587-4]
DR Antibodypedia; 316; 76 antibodies from 18 providers.
DR DNASU; 7625; -.
DR Ensembl; ENST00000400451.7; ENSP00000383301.2; ENSG00000185252.19. [Q16587-1]
DR Ensembl; ENST00000403682.7; ENSP00000384750.3; ENSG00000185252.19. [Q16587-5]
DR Ensembl; ENST00000405993.2; ENSP00000385855.1; ENSG00000185252.19. [Q16587-3]
DR Ensembl; ENST00000611540.4; ENSP00000483077.1; ENSG00000185252.19. [Q16587-1]
DR GeneID; 7625; -.
DR KEGG; hsa:7625; -.
DR MANE-Select; ENST00000400451.7; ENSP00000383301.2; NM_003426.4; NP_003417.2.
DR UCSC; uc002zsh.5; human. [Q16587-1]
DR CTD; 7625; -.
DR DisGeNET; 7625; -.
DR GeneCards; ZNF74; -.
DR HGNC; HGNC:13144; ZNF74.
DR HPA; ENSG00000185252; Low tissue specificity.
DR MIM; 194548; gene.
DR neXtProt; NX_Q16587; -.
DR OpenTargets; ENSG00000185252; -.
DR PharmGKB; PA37718; -.
DR VEuPathDB; HostDB:ENSG00000185252; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162000; -.
DR HOGENOM; CLU_002678_44_5_1; -.
DR InParanoid; Q16587; -.
DR OMA; GGPCPEW; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q16587; -.
DR TreeFam; TF341817; -.
DR PathwayCommons; Q16587; -.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR SignaLink; Q16587; -.
DR BioGRID-ORCS; 7625; 27 hits in 1096 CRISPR screens.
DR GeneWiki; ZNF74; -.
DR GenomeRNAi; 7625; -.
DR Pharos; Q16587; Tbio.
DR PRO; PR:Q16587; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q16587; protein.
DR Bgee; ENSG00000185252; Expressed in cortical plate and 127 other tissues.
DR ExpressionAtlas; Q16587; baseline and differential.
DR Genevisible; Q16587; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
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:0003723; F:RNA 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:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:ProtInc.
DR CDD; cd07765; KRAB_A-box; 1.
DR InterPro; IPR001909; KRAB.
DR InterPro; IPR036051; KRAB_dom_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF01352; KRAB; 1.
DR Pfam; PF00096; zf-C2H2; 8.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 12.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 6.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 12.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 12.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW Reference proteome; Repeat; RNA-binding; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..644
FT /note="Zinc finger protein 74"
FT /id="PRO_0000047383"
FT DOMAIN 43..114
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 248..270
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 276..298
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 304..326
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 332..354
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 360..382
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 388..410
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 416..438
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 444..466
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 472..494
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 500..522
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 528..550
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 556..578
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT CROSSLNK 582
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..82
FT /note="MEIPAPEPEKTALSSQDPALSLKENLEDISGWGLPEARSKESVSFKDVAVDF
FT TQEEWGQLDSPQRALYRDVMLENYQNLLAL -> MPSPPFSPRA (in isoform
FT 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_006893"
FT VAR_SEQ 1..71
FT /note="Missing (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:8268910, ECO:0000303|PubMed:8663113"
FT /id="VSP_006891"
FT VAR_SEQ 12..178
FT /note="ALSSQDPALSLKENLEDISGWGLPEARSKESVSFKDVAVDFTQEEWGQLDSP
FT QRALYRDVMLENYQNLLALGPPLHKPDVISHLERGEEPWSMQREVPRGPCPEWELKAVP
FT SQQQGICKEEPAQEPIMERPLGGAQAWGRQAGALQRSQAAPWAPAPAMVWDVPVEE ->
FT GIGEFQGCGCGLHPGGVGSTRLPSEGLVPGCDVGELPEPSCPRTSTAQARCDLSSGTRR
FT GAMEHAEGSPQRALSRMGAEGGALSTAGHLQRRTGPGAHHGAAPRRGAGVGAPGRCSAE
FT ESGCALGARTCHGLGRPCRGIPPQVSPLRPATRSRGGTLAGHTQERPGH (in
FT isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_045530"
FT VAR_SEQ 83..114
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_006892"
FT VAR_SEQ 179..644
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_045531"
FT VARIANT 117
FT /note="E -> K (in dbSNP:rs3747076)"
FT /evidence="ECO:0000269|PubMed:11705709,
FT ECO:0000269|PubMed:14702039"
FT /id="VAR_012993"
FT VARIANT 623..624
FT /note="KL -> NF"
FT /id="VAR_012994"
FT CONFLICT 171
FT /note="V -> A (in Ref. 7; AAH13395)"
FT /evidence="ECO:0000305"
FT CONFLICT 517
FT /note="V -> M (in Ref. 1; CAA63379, 2; CAA50632 and 4;
FT AAF21777/AAF21778/AAF21779/AAF21780)"
FT /evidence="ECO:0000305"
FT CONFLICT 569
FT /note="S -> P (in Ref. 5; BAH13068)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 644 AA; 72207 MW; 87E5AA122BBC82F1 CRC64;
MEIPAPEPEK TALSSQDPAL SLKENLEDIS GWGLPEARSK ESVSFKDVAV DFTQEEWGQL
DSPQRALYRD VMLENYQNLL ALGPPLHKPD VISHLERGEE PWSMQREVPR GPCPEWELKA
VPSQQQGICK EEPAQEPIME RPLGGAQAWG RQAGALQRSQ AAPWAPAPAM VWDVPVEEFP
LRCPLFAQQR VPEGGPLLDT RKNVQATEGR TKAPARLCAG ENASTPSEPE KFPQVRRQRG
AGAGEGEFVC GECGKAFRQS SSLTLHRRWH SREKAYKCDE CGKAFTWSTN LLEHRRIHTG
EKPFFCGECG KAFSCHSSLN VHQRIHTGER PYKCSACEKA FSCSSLLSMH LRVHTGEKPY
RCGECGKAFN QRTHLTRHHR IHTGEKPYQC GSCGKAFTCH SSLTVHEKIH SGDKPFKCSD
CEKAFNSRSR LTLHQRTHTG EKPFKCADCG KGFSCHAYLL VHRRIHSGEK PFKCNECGKA
FSSHAYLIVH RRIHTGEKPF DCSQCWKAFS CHSSLIVHQR IHTGEKPYKC SECGRAFSQN
HCLIKHQKIH SGEKSFKCEK CGEMFNWSSH LTEHQRLHSE GKPLAIQFNK HLLSTYYVPG
SLLGAGDAGL RDVDPIDALD VAKLLCVVPP RAGRNFSLGS KPRN
