CIR1_HUMAN
ID CIR1_HUMAN Reviewed; 450 AA.
AC Q86X95; A6NFI6; A8K8M4; O95367; Q12804; Q4G1B9; Q6PJI4; Q8IWI2;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Corepressor interacting with RBPJ 1;
DE AltName: Full=CBF1-interacting corepressor;
DE AltName: Full=Recepin;
GN Name=CIR1; Synonyms=CIR;
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, INTERACTION WITH RBPJ;
RP SAP30 AND HDAC2, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=9874765; DOI=10.1073/pnas.96.1.23;
RA Hsieh J.J.-D., Zhou S., Chen L., Young D.B., Hayward S.D.;
RT "CIR, a corepressor linking the DNA binding factor CBF1 to the histone
RT deacetylase complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:23-28(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RA Chai K.X., Li L., Chao J., Chao L.;
RL Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Eye, Lymph, Testis, and Uterus;
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 INTERACTION WITH SNW1.
RX PubMed=10644367; DOI=10.1128/jvi.74.4.1939-1947.2000;
RA Zhou S., Fujimuro M., Hsieh J.J., Chen L., Hayward S.D.;
RT "A role for SKIP in EBNA2 activation of CBF1-repressed promoters.";
RL J. Virol. 74:1939-1947(2000).
RN [7]
RP INTERACTION WITH EPSTEIN-BARR VIRUS RPMS1, AND SUBCELLULAR LOCATION.
RX PubMed=11222720; DOI=10.1128/jvi.75.6.2946-2956.2001;
RA Zhang J., Chen H., Weinmaster G., Hayward S.D.;
RT "Epstein-Barr virus BamHi-a rightward transcript-encoded RPMS protein
RT interacts with the CBF1-associated corepressor CIR to negatively regulate
RT the activity of EBNA2 and NotchIC.";
RL J. Virol. 75:2946-2956(2001).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP FUNCTION, AND INTERACTION WITH NKAP.
RX PubMed=19409814; DOI=10.1016/j.immuni.2009.02.011;
RA Pajerowski A.G., Nguyen C., Aghajanian H., Shapiro M.J., Shapiro V.S.;
RT "NKAP is a transcriptional repressor of notch signaling and is required for
RT T cell development.";
RL Immunity 30:696-707(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP SUBCELLULAR LOCATION, INTERACTION WITH NEK6, AND PHOSPHORYLATION.
RX PubMed=20873783; DOI=10.1021/pr100562w;
RA Vaz Meirelles G., Ferreira Lanza D.C., da Silva J.C., Santana Bernachi J.,
RA Paes Leme A.F., Kobarg J.;
RT "Characterization of hNek6 interactome reveals an important role for its
RT short N-terminal domain and colocalization with proteins at the
RT centrosome.";
RL J. Proteome Res. 9:6298-6316(2010).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [15]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-79 AND LYS-340, AND
RP IDENTIFICATION BY MASS 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).
CC -!- FUNCTION: May modulate splice site selection during alternative
CC splicing of pre-mRNAs (By similarity). Regulates transcription and acts
CC as corepressor for RBPJ. Recruits RBPJ to the Sin3-histone deacetylase
CC complex (HDAC). Required for RBPJ-mediated repression of transcription.
CC {ECO:0000250, ECO:0000269|PubMed:19409814, ECO:0000269|PubMed:9874765}.
CC -!- SUBUNIT: Interacts with RP9, SNW1, SFRS1, SFRS2,U2AF1, RBPJ, SAP30,
CC HDAC2 NKAP and NEK6. Interacts with Epstein-Barr virus RPMS1. Component
CC of the histone deacetylase complex. Component of the Notch corepressor
CC complex. Interacts with NKAPL (By similarity).
CC {ECO:0000250|UniProtKB:Q9DA19, ECO:0000269|PubMed:10644367,
CC ECO:0000269|PubMed:11222720, ECO:0000269|PubMed:19409814,
CC ECO:0000269|PubMed:20873783, ECO:0000269|PubMed:9874765}.
CC -!- INTERACTION:
CC Q86X95; Q8TAP6: CEP76; NbExp=3; IntAct=EBI-627102, EBI-742887;
CC Q86X95; Q07955: SRSF1; NbExp=3; IntAct=EBI-627102, EBI-398920;
CC Q86X95; Q01130: SRSF2; NbExp=4; IntAct=EBI-627102, EBI-627047;
CC Q86X95; Q01081: U2AF1; NbExp=4; IntAct=EBI-627102, EBI-632461;
CC Q86X95-2; Q7L190: DPPA4; NbExp=3; IntAct=EBI-12034850, EBI-710457;
CC Q86X95-2; Q8IYB1: MB21D2; NbExp=3; IntAct=EBI-12034850, EBI-11323212;
CC -!- SUBCELLULAR LOCATION: Nucleus speckle. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome. Note=Colocalizes with NEK6
CC in the centrosome.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q86X95-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86X95-2; Sequence=VSP_020091, VSP_020092;
CC -!- TISSUE SPECIFICITY: Highly expressed in heart, brain, placenta, liver,
CC skeletal muscle and pancreas. {ECO:0000269|PubMed:9874765}.
CC -!- PTM: Phosphorylated by NEK6. {ECO:0000269|PubMed:20873783}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA17853.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAH21175.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAH38987.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AF098297; AAD05243.1; -; mRNA.
DR EMBL; U03644; AAA17853.1; ALT_FRAME; mRNA.
DR EMBL; AK292389; BAF85078.1; -; mRNA.
DR EMBL; AC018470; AAY24216.1; -; Genomic_DNA.
DR EMBL; BC015040; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC021175; AAH21175.1; ALT_SEQ; mRNA.
DR EMBL; BC038987; AAH38987.1; ALT_SEQ; mRNA.
DR EMBL; BC046098; AAH46098.1; -; mRNA.
DR CCDS; CCDS2256.1; -. [Q86X95-1]
DR PIR; G01227; G01227.
DR RefSeq; NP_004873.3; NM_004882.3. [Q86X95-1]
DR PDB; 6ZYM; EM; 3.40 A; 9=1-450.
DR PDBsum; 6ZYM; -.
DR AlphaFoldDB; Q86X95; -.
DR SMR; Q86X95; -.
DR BioGRID; 114916; 66.
DR IntAct; Q86X95; 31.
DR MINT; Q86X95; -.
DR STRING; 9606.ENSP00000339723; -.
DR iPTMnet; Q86X95; -.
DR PhosphoSitePlus; Q86X95; -.
DR BioMuta; CIR1; -.
DR DMDM; 74727790; -.
DR EPD; Q86X95; -.
DR jPOST; Q86X95; -.
DR MassIVE; Q86X95; -.
DR MaxQB; Q86X95; -.
DR PaxDb; Q86X95; -.
DR PeptideAtlas; Q86X95; -.
DR PRIDE; Q86X95; -.
DR ProteomicsDB; 70256; -. [Q86X95-1]
DR ProteomicsDB; 70257; -. [Q86X95-2]
DR Antibodypedia; 19463; 142 antibodies from 24 providers.
DR DNASU; 9541; -.
DR Ensembl; ENST00000342016.8; ENSP00000339723.3; ENSG00000138433.16. [Q86X95-1]
DR GeneID; 9541; -.
DR KEGG; hsa:9541; -.
DR MANE-Select; ENST00000342016.8; ENSP00000339723.3; NM_004882.4; NP_004873.3.
DR UCSC; uc002uim.4; human. [Q86X95-1]
DR CTD; 9541; -.
DR DisGeNET; 9541; -.
DR GeneCards; CIR1; -.
DR HGNC; HGNC:24217; CIR1.
DR HPA; ENSG00000138433; Low tissue specificity.
DR MIM; 605228; gene.
DR neXtProt; NX_Q86X95; -.
DR OpenTargets; ENSG00000138433; -.
DR PharmGKB; PA165696415; -.
DR VEuPathDB; HostDB:ENSG00000138433; -.
DR eggNOG; KOG3794; Eukaryota.
DR GeneTree; ENSGT00730000111135; -.
DR HOGENOM; CLU_035642_2_0_1; -.
DR InParanoid; Q86X95; -.
DR OMA; HKKKHES; -.
DR OrthoDB; 1604301at2759; -.
DR PhylomeDB; Q86X95; -.
DR TreeFam; TF317567; -.
DR PathwayCommons; Q86X95; -.
DR SignaLink; Q86X95; -.
DR SIGNOR; Q86X95; -.
DR BioGRID-ORCS; 9541; 93 hits in 1047 CRISPR screens.
DR ChiTaRS; CIR1; human.
DR GeneWiki; CIR_(gene); -.
DR GenomeRNAi; 9541; -.
DR Pharos; Q86X95; Tdark.
DR PRO; PR:Q86X95; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q86X95; protein.
DR Bgee; ENSG00000138433; Expressed in tendon of biceps brachii and 205 other tissues.
DR ExpressionAtlas; Q86X95; baseline and differential.
DR Genevisible; Q86X95; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0042826; F:histone deacetylase binding; IDA:MGI.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:UniProtKB.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR InterPro; IPR040014; CIR1.
DR InterPro; IPR019339; CIR_N_dom.
DR PANTHER; PTHR13151; PTHR13151; 1.
DR Pfam; PF10197; Cir_N; 1.
DR SMART; SM01083; Cir_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Cytoskeleton;
KW Isopeptide bond; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..450
FT /note="Corepressor interacting with RBPJ 1"
FT /id="PRO_0000247984"
FT REGION 1..121
FT /note="Interaction with RBPJ"
FT /evidence="ECO:0000269|PubMed:9874765"
FT REGION 72..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..232
FT /note="Interaction with RP9"
FT /evidence="ECO:0000250"
FT REGION 218..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 235..245
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 291..298
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 77..93
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..258
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..278
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..450
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT CROSSLNK 79
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 340
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 162..202
FT /note="GPSMHPSELIAEMRNSGFALKRNVLGRNLTANDPSQEYVAS -> DAVLQIE
FT GFWAIDAPLGANSGDEKQWVCTETKCTGEKLDRK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020091"
FT VAR_SEQ 203..450
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020092"
FT CONFLICT 48
FT /note="K -> R (in Ref. 1; AAD05243)"
FT /evidence="ECO:0000305"
FT CONFLICT 113
FT /note="N -> S (in Ref. 1; AAD05243)"
FT /evidence="ECO:0000305"
FT CONFLICT 172
FT /note="A -> G (in Ref. 2; AAA17853)"
FT /evidence="ECO:0000305"
FT CONFLICT 325
FT /note="S -> T (in Ref. 1; AAD05243 and 2; AAA17853)"
FT /evidence="ECO:0000305"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:6ZYM"
SQ SEQUENCE 450 AA; 52313 MW; 5D0C1CBD9C87569D CRC64;
MGKSFANFMC KKDFHPASKS NIKKVWMAEQ KISYDKKKQE ELMQQYLKEQ ESYDNRLLMG
DERVKNGLNF MYEAPPGAKK ENKEKEETEG ETEYKFEWQK GAPREKYAKD DMNIRDQPFG
IQVRNVRCIK CHKWGHVNTD RECPLFGLSG INASSVPTDG SGPSMHPSEL IAEMRNSGFA
LKRNVLGRNL TANDPSQEYV ASEGEEDPEV EFLKSLTTKQ KQKLLRKLDR LEKKKKKKDR
KKKKFQKSRS KHKKHKSSSS SSSSSSSSSS TETSESSSES ESNNKEKKIQ RKKRKKNKCS
GHNNSDSEEK DKSKKRKLHE ELSSSHHNRE KAKEKPRFLK HESSREDSKW SHSDSDKKSR
THKHSPEKRG SERKEGSSRS HGREERSRRS RSRSPGSYKQ RETRKRAQRN PGEEQSRRND
SRSHGTDLYR GEKMYREHPG GTHTKVTQRE
