KHDC4_HUMAN
ID KHDC4_HUMAN Reviewed; 614 AA.
AC Q7Z7F0; O94981; Q7L7Q2; Q7Z7E9; Q8TBQ0;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=KH homology domain-containing protein 4 {ECO:0000312|HGNC:HGNC:29145};
DE AltName: Full=Brings lots of money 7 {ECO:0000303|PubMed:19641227};
DE AltName: Full=Pre-mRNA splicing factor protein KHDC4 {ECO:0000305};
GN Name=KHDC4 {ECO:0000312|HGNC:HGNC:29145};
GN Synonyms=BLOM7 {ECO:0000303|PubMed:19641227}, KIAA0907,
GN SNORA80EHG {ECO:0000312|HGNC:HGNC:29145};
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] (ISOFORMS 1; 2 AND 3), FUNCTION, SUBCELLULAR
RP LOCATION, SUBUNIT, ALTERNATIVE SPLICING, DOMAIN, TISSUE SPECIFICITY,
RP INTERACTION WITH PRPF19, AND INTERACTION WITH U2AF65 (ISOFORM 2).
RX PubMed=19641227; DOI=10.1074/jbc.m109.036632;
RA Grillari J., Loescher M., Denegri M., Lee K., Fortschegger K.,
RA Eisenhaber F., Ajuh P., Lamond A.I., Katinger H., Grillari-Voglauer R.;
RT "Blom7alpha is a novel heterogeneous nuclear ribonucleoprotein K homology
RT domain protein involved in pre-mRNA splicing that interacts with SNEVPrp19-
RT Pso4.";
RL J. Biol. Chem. 284:29193-29204(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=10048485; DOI=10.1093/dnares/5.6.355;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:355-364(1998).
RN [3]
RP SEQUENCE REVISION.
RA Ohara O., Suyama M., Kikuno R., Nagase T., Ishikawa K.;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
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] (ISOFORMS 1 AND 4).
RC TISSUE=Adrenal cortex, and Lymph;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-571 AND SER-572, AND
RP IDENTIFICATION BY 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-571 AND SER-572, AND
RP IDENTIFICATION BY 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 [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=23144703; DOI=10.1371/journal.pone.0047497;
RA Loescher M., Schosserer M., Dausse E., Lee K., Ajuh P.,
RA Grillari-Voglauer R., Lamond A.I., Toulme J.J., Grillari J.;
RT "Inhibition of pre-mRNA splicing by a synthetic Blom7alpha-interacting
RT small RNA.";
RL PLoS ONE 7:E47497-E47497(2012).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [10]
RP STRUCTURE BY NMR OF 227-338.
RG RIKEN structural genomics initiative (RSGI);
RT "solution structure of the KH domain in KIAA0907 protein.";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- FUNCTION: RNA-binding protein involved in pre-mRNA splicing
CC (PubMed:19641227). Interacts with the PRP19C/Prp19 complex/NTC/Nineteen
CC complex which is part of the spliceosome (PubMed:19641227). Involved in
CC regulating splice site selection (PubMed:19641227). Binds
CC preferentially RNA with A/C rich sequences and poly-C stretches
CC (PubMed:23144703). {ECO:0000269|PubMed:19641227,
CC ECO:0000269|PubMed:23144703}.
CC -!- SUBUNIT: Interacts with PRPF19 (PubMed:19641227).
CC {ECO:0000269|PubMed:19641227}.
CC -!- SUBUNIT: [Isoform 2]: Interacts with U2AF65 (PubMed:19641227).
CC {ECO:0000269|PubMed:19641227}.
CC -!- INTERACTION:
CC Q7Z7F0; Q9UHX1: PUF60; NbExp=3; IntAct=EBI-751942, EBI-1053259;
CC Q7Z7F0; Q14498: RBM39; NbExp=3; IntAct=EBI-751942, EBI-395290;
CC Q7Z7F0; Q14498-3: RBM39; NbExp=3; IntAct=EBI-751942, EBI-6654703;
CC Q7Z7F0; Q15637: SF1; NbExp=5; IntAct=EBI-751942, EBI-744603;
CC Q7Z7F0-4; Q8N9N5-2: BANP; NbExp=3; IntAct=EBI-9089060, EBI-11524452;
CC Q7Z7F0-4; Q9NWQ9: C14orf119; NbExp=3; IntAct=EBI-9089060, EBI-725606;
CC Q7Z7F0-4; P22607: FGFR3; NbExp=3; IntAct=EBI-9089060, EBI-348399;
CC Q7Z7F0-4; Q14957: GRIN2C; NbExp=3; IntAct=EBI-9089060, EBI-8285963;
CC Q7Z7F0-4; P06396: GSN; NbExp=3; IntAct=EBI-9089060, EBI-351506;
CC Q7Z7F0-4; Q9Y2W7: KCNIP3; NbExp=3; IntAct=EBI-9089060, EBI-751501;
CC Q7Z7F0-4; P43365: MAGEA12; NbExp=3; IntAct=EBI-9089060, EBI-749530;
CC Q7Z7F0-4; Q16656-4: NRF1; NbExp=3; IntAct=EBI-9089060, EBI-11742836;
CC Q7Z7F0-4; P61970: NUTF2; NbExp=3; IntAct=EBI-9089060, EBI-591778;
CC Q7Z7F0-4; Q9HB75-2: PIDD1; NbExp=3; IntAct=EBI-9089060, EBI-12326369;
CC Q7Z7F0-4; O43741: PRKAB2; NbExp=3; IntAct=EBI-9089060, EBI-1053424;
CC Q7Z7F0-4; Q9NZ81: PRR13; NbExp=3; IntAct=EBI-9089060, EBI-740924;
CC Q7Z7F0-4; P20618: PSMB1; NbExp=3; IntAct=EBI-9089060, EBI-372273;
CC Q7Z7F0-4; Q9UHX1-2: PUF60; NbExp=10; IntAct=EBI-9089060, EBI-11529177;
CC Q7Z7F0-4; Q9UHX1-5: PUF60; NbExp=3; IntAct=EBI-9089060, EBI-11526420;
CC Q7Z7F0-4; Q9UHX1-6: PUF60; NbExp=3; IntAct=EBI-9089060, EBI-11085298;
CC Q7Z7F0-4; Q2TAL8: QRICH1; NbExp=3; IntAct=EBI-9089060, EBI-2798044;
CC Q7Z7F0-4; Q14498-3: RBM39; NbExp=3; IntAct=EBI-9089060, EBI-6654703;
CC Q7Z7F0-4; Q9BQY4: RHOXF2; NbExp=3; IntAct=EBI-9089060, EBI-372094;
CC Q7Z7F0-4; P21673: SAT1; NbExp=3; IntAct=EBI-9089060, EBI-711613;
CC Q7Z7F0-4; Q5MJ10: SPANXN2; NbExp=3; IntAct=EBI-9089060, EBI-12023934;
CC Q7Z7F0-4; P26368-2: U2AF2; NbExp=3; IntAct=EBI-9089060, EBI-11097439;
CC Q7Z7F0-4; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-9089060, EBI-741480;
CC Q7Z7F0-4; Q15696: ZRSR2; NbExp=3; IntAct=EBI-9089060, EBI-6657923;
CC Q7Z7F0-4; B2RDP1; NbExp=3; IntAct=EBI-9089060, EBI-18956102;
CC Q7Z7F0-4; Q9Y649; NbExp=3; IntAct=EBI-9089060, EBI-25900580;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19641227,
CC ECO:0000269|PubMed:23144703}. Cytoplasm {ECO:0000269|PubMed:19641227}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=Alpha, Blom7alpha {ECO:0000303|PubMed:19641227};
CC IsoId=Q7Z7F0-1; Sequence=Displayed;
CC Name=2; Synonyms=Beta, KIAA0907 {ECO:0000303|PubMed:19641227};
CC IsoId=Q7Z7F0-2; Sequence=VSP_027242, VSP_027243;
CC Name=3; Synonyms=Gamma;
CC IsoId=Q7Z7F0-3; Sequence=VSP_027240, VSP_027241;
CC Name=4;
CC IsoId=Q7Z7F0-4; Sequence=VSP_027238, VSP_027239;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Expressed at high level in skeletal
CC muscle, kidney, heart, brain and liver. {ECO:0000269|PubMed:19641227}.
CC -!- DOMAIN: The C-terminal part is necessary for the interaction with the
CC PRP19C/Prp19 complex/NTC/Nineteen complex.
CC {ECO:0000269|PubMed:19641227}.
CC -!- DOMAIN: The KH domains mediate RNA-binding.
CC {ECO:0000269|PubMed:23144703}.
CC -!- MISCELLANEOUS: [Isoform 2]: Interacts with U2AF65.
CC {ECO:0000269|PubMed:19641227}.
CC -!- SIMILARITY: Belongs to the KHDC4 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA74930.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY112680; AAM51855.1; -; mRNA.
DR EMBL; AY112681; AAM51856.1; -; mRNA.
DR EMBL; AY112682; AAM51857.1; -; mRNA.
DR EMBL; AB020714; BAA74930.2; ALT_INIT; mRNA.
DR EMBL; AL355388; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC027182; AAH27182.1; -; mRNA.
DR EMBL; BC062637; AAH62637.1; -; mRNA.
DR CCDS; CCDS30885.1; -. [Q7Z7F0-1]
DR RefSeq; NP_055764.2; NM_014949.3. [Q7Z7F0-1]
DR PDB; 2YQR; NMR; -; A=227-338.
DR PDBsum; 2YQR; -.
DR AlphaFoldDB; Q7Z7F0; -.
DR SMR; Q7Z7F0; -.
DR BioGRID; 116555; 51.
DR IntAct; Q7Z7F0; 40.
DR MINT; Q7Z7F0; -.
DR STRING; 9606.ENSP00000357304; -.
DR iPTMnet; Q7Z7F0; -.
DR PhosphoSitePlus; Q7Z7F0; -.
DR BioMuta; KHDC4; -.
DR DMDM; 74750236; -.
DR EPD; Q7Z7F0; -.
DR jPOST; Q7Z7F0; -.
DR MassIVE; Q7Z7F0; -.
DR MaxQB; Q7Z7F0; -.
DR PaxDb; Q7Z7F0; -.
DR PeptideAtlas; Q7Z7F0; -.
DR PRIDE; Q7Z7F0; -.
DR ProteomicsDB; 69525; -. [Q7Z7F0-1]
DR ProteomicsDB; 69526; -. [Q7Z7F0-2]
DR ProteomicsDB; 69527; -. [Q7Z7F0-3]
DR ProteomicsDB; 69528; -. [Q7Z7F0-4]
DR Antibodypedia; 1657; 90 antibodies from 21 providers.
DR DNASU; 22889; -.
DR Ensembl; ENST00000368319.3; ENSP00000357302.3; ENSG00000132680.11. [Q7Z7F0-3]
DR Ensembl; ENST00000368320.7; ENSP00000357303.3; ENSG00000132680.11. [Q7Z7F0-2]
DR Ensembl; ENST00000368321.8; ENSP00000357304.3; ENSG00000132680.11. [Q7Z7F0-1]
DR GeneID; 22889; -.
DR KEGG; hsa:22889; -.
DR MANE-Select; ENST00000368321.8; ENSP00000357304.3; NM_014949.4; NP_055764.2.
DR UCSC; uc001fmi.2; human. [Q7Z7F0-1]
DR CTD; 22889; -.
DR DisGeNET; 22889; -.
DR GeneCards; KHDC4; -.
DR HGNC; HGNC:29145; KHDC4.
DR HPA; ENSG00000132680; Low tissue specificity.
DR MIM; 619370; gene.
DR neXtProt; NX_Q7Z7F0; -.
DR OpenTargets; ENSG00000132680; -.
DR PharmGKB; PA142671618; -.
DR VEuPathDB; HostDB:ENSG00000132680; -.
DR eggNOG; KOG1960; Eukaryota.
DR GeneTree; ENSGT00510000047412; -.
DR HOGENOM; CLU_032219_1_0_1; -.
DR InParanoid; Q7Z7F0; -.
DR OMA; MSFCGTQ; -.
DR OrthoDB; 633868at2759; -.
DR PhylomeDB; Q7Z7F0; -.
DR PathwayCommons; Q7Z7F0; -.
DR SignaLink; Q7Z7F0; -.
DR BioGRID-ORCS; 22889; 36 hits in 1082 CRISPR screens.
DR ChiTaRS; KIAA0907; human.
DR EvolutionaryTrace; Q7Z7F0; -.
DR GenomeRNAi; 22889; -.
DR Pharos; Q7Z7F0; Tdark.
DR PRO; PR:Q7Z7F0; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q7Z7F0; protein.
DR Bgee; ENSG00000132680; Expressed in tibia and 207 other tissues.
DR Genevisible; Q7Z7F0; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0006376; P:mRNA splice site selection; IDA:UniProtKB.
DR Gene3D; 3.30.1370.10; -; 2.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR InterPro; IPR031121; RIK/BLOM7.
DR PANTHER; PTHR15744; PTHR15744; 1.
DR SUPFAM; SSF54791; SSF54791; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; RNA-binding.
FT CHAIN 1..614
FT /note="KH homology domain-containing protein 4"
FT /id="PRO_0000296669"
FT DOMAIN 100..180
FT /note="KH 1"
FT /evidence="ECO:0000305|PubMed:23144703"
FT DOMAIN 235..317
FT /note="KH 2"
FT /evidence="ECO:0000305|PubMed:23144703"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 480..549
FT /note="Required for nuclear retention"
FT /evidence="ECO:0000269|PubMed:23144703"
FT REGION 567..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..456
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..504
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..606
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 571
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 572
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT VAR_SEQ 228..241
FT /note="MHYVQDKLFVGLEH -> VCFGEGSLIALSFL (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027238"
FT VAR_SEQ 242..614
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027239"
FT VAR_SEQ 338..378
FT /note="GYTQPSAISSVPPQPPYYPSNGYQSGYPVVPPPQQPVQPPY -> AASSTSL
FT RSTKHSATSCFISTWSLAGITYWSPTCANTIPDNTSAASS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:19641227"
FT /id="VSP_027240"
FT VAR_SEQ 379..614
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:19641227"
FT /id="VSP_027241"
FT VAR_SEQ 549..564
FT /note="DYPAKKMKTTEKGFGL -> GECDIAGGTGEWLRLV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10048485,
FT ECO:0000303|PubMed:19641227"
FT /id="VSP_027242"
FT VAR_SEQ 565..614
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10048485,
FT ECO:0000303|PubMed:19641227"
FT /id="VSP_027243"
FT STRAND 231..236
FT /evidence="ECO:0007829|PDB:2YQR"
FT TURN 244..246
FT /evidence="ECO:0007829|PDB:2YQR"
FT HELIX 248..252
FT /evidence="ECO:0007829|PDB:2YQR"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:2YQR"
FT HELIX 258..267
FT /evidence="ECO:0007829|PDB:2YQR"
FT STRAND 270..276
FT /evidence="ECO:0007829|PDB:2YQR"
FT TURN 283..285
FT /evidence="ECO:0007829|PDB:2YQR"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:2YQR"
FT STRAND 294..301
FT /evidence="ECO:0007829|PDB:2YQR"
FT HELIX 302..330
FT /evidence="ECO:0007829|PDB:2YQR"
SQ SEQUENCE 614 AA; 64845 MW; 61968993DA061561 CRC64;
MSAGSATHPG AGGRRSKWDQ PAPAPLLFLP PAAPGGEVTS SGGSPGGTTA APSGALDAAA
AVAAKINAML MAKGKLKPTQ NASEKLQAPG KGLTSNKSKD DLVVAEVEIN DVPLTCRNLL
TRGQTQDEIS RLSGAAVSTR GRFMTTEEKA KVGPGDRPLY LHVQGQTREL VDRAVNRIKE
IITNGVVKAA TGTSPTFNGA TVTVYHQPAP IAQLSPAVSQ KPPFQSGMHY VQDKLFVGLE
HAVPTFNVKE KVEGPGCSYL QHIQIETGAK VFLRGKGSGC IEPASGREAF EPMYIYISHP
KPEGLAAAKK LCENLLQTVH AEYSRFVNQI NTAVPLPGYT QPSAISSVPP QPPYYPSNGY
QSGYPVVPPP QQPVQPPYGV PSIVPPAVSL APGVLPALPT GVPPVPTQYP ITQVQPPAST
GQSPMGGPFI PAAPVKTALP AGPQPQPQPQ PPLPSQPQAQ KRRFTEELPD ERESGLLGYQ
HGPIHMTNLG TGFSSQNEIE GAGSKPASSS GKERERDRQL MPPPAFPVTG IKTESDERNG
SGTLTGSHDY PAKKMKTTEK GFGLVAYAAD SSDEEEEHGG HKNASSFPQG WSLGYQYPSS
QPRAKQQMPF WMAP