ID MORC4_HUMAN Reviewed; 937 AA.
AC Q8TE76; A1YR23; A1YR24; H7BXF1; Q5JUK7; Q96MZ2; Q9HAI7;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 24-JAN-2024, entry version 160.
DE RecName: Full=MORC family CW-type zinc finger protein 4;
DE AltName: Full=Zinc finger CW-type coiled-coil domain protein 2;
DE AltName: Full=Zinc finger CW-type domain protein 4;
GN Name=MORC4; Synonyms=ZCW4, ZCWCC2;
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 2 AND 3), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND ALTERNATIVE SPLICING.
RC TISSUE=Testis;
RX PubMed=17608765; DOI=10.1111/j.1365-2141.2007.06680.x;
RA Liggins A.P., Cooper C.D., Lawrie C.H., Brown P.J., Collins G.P.,
RA Hatton C.S., Pulford K., Banham A.H.;
RT "MORC4, a novel member of the MORC family, is highly expressed in a subset
RT of diffuse large B-cell lymphomas.";
RL Br. J. Haematol. 138:479-486(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 172-937 (ISOFORM 1), AND VARIANT
RP ILE-473.
RC TISSUE=Embryo;
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 FUNCTION, AND DOMAIN CW-TYPE ZINC FINGER.
RX PubMed=26933034; DOI=10.1074/jbc.m116.718973;
RA Liu Y., Tempel W., Zhang Q., Liang X., Loppnau P., Qin S., Min J.;
RT "Family-wide Characterization of Histone Binding Abilities of Human CW
RT Domain-containing Proteins.";
RL J. Biol. Chem. 291:9000-9013(2016).
CC -!- FUNCTION: Histone methylation reader which binds to non-methylated
CC (H3K4me0), monomethylated (H3K4me1), dimethylated (H3K4me2) and
CC trimethylated (H3K4me3) 'Lys-4' on histone H3 (PubMed:26933034). The
CC order of binding preference is H3K4me3 > H3K4me2 > H3K4me1 > H3K4me0
CC (PubMed:26933034). {ECO:0000269|PubMed:26933034}.
CC -!- INTERACTION:
CC Q8TE76; P40763: STAT3; NbExp=2; IntAct=EBI-3940432, EBI-518675;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:17608765}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8TE76-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TE76-2; Sequence=VSP_045025, VSP_045026;
CC Name=3;
CC IsoId=Q8TE76-3; Sequence=VSP_045026;
CC -!- TISSUE SPECIFICITY: Expressed at low levels in normal tissues, with
CC highest expression levels in placenta and testis. Expression is
CC significantly increased in subset of diffuse large B-cell lymphomas.
CC {ECO:0000269|PubMed:17608765}.
CC -!- DOMAIN: The CW-TYPE zinc finger mediates its binding to trimethylated
CC histone H3K4me3. {ECO:0000269|PubMed:26933034}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB13859.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB71125.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; EF125209; ABL84747.1; -; mRNA.
DR EMBL; EF125210; ABL84748.1; -; mRNA.
DR EMBL; AL158821; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK021627; BAB13859.1; ALT_INIT; mRNA.
DR EMBL; AK056235; BAB71125.1; ALT_INIT; mRNA.
DR CCDS; CCDS14525.2; -. [Q8TE76-1]
DR CCDS; CCDS48146.1; -. [Q8TE76-3]
DR RefSeq; NP_001078823.1; NM_001085354.2. [Q8TE76-3]
DR RefSeq; NP_078933.3; NM_024657.4. [Q8TE76-1]
DR PDB; 7K7T; X-ray; 2.94 A; A/B=29-486.
DR PDBsum; 7K7T; -.
DR AlphaFoldDB; Q8TE76; -.
DR SMR; Q8TE76; -.
DR BioGRID; 122827; 66.
DR IntAct; Q8TE76; 43.
DR MINT; Q8TE76; -.
DR STRING; 9606.ENSP00000347821; -.
DR iPTMnet; Q8TE76; -.
DR PhosphoSitePlus; Q8TE76; -.
DR BioMuta; MORC4; -.
DR DMDM; 73920232; -.
DR EPD; Q8TE76; -.
DR jPOST; Q8TE76; -.
DR MassIVE; Q8TE76; -.
DR MaxQB; Q8TE76; -.
DR PaxDb; 9606-ENSP00000347821; -.
DR PeptideAtlas; Q8TE76; -.
DR ProteomicsDB; 163; -.
DR ProteomicsDB; 43259; -.
DR ProteomicsDB; 74413; -. [Q8TE76-1]
DR Pumba; Q8TE76; -.
DR Antibodypedia; 386; 42 antibodies from 11 providers.
DR DNASU; 79710; -.
DR Ensembl; ENST00000255495.7; ENSP00000255495.7; ENSG00000133131.15. [Q8TE76-3]
DR Ensembl; ENST00000355610.9; ENSP00000347821.4; ENSG00000133131.15. [Q8TE76-1]
DR GeneID; 79710; -.
DR KEGG; hsa:79710; -.
DR MANE-Select; ENST00000355610.9; ENSP00000347821.4; NM_024657.5; NP_078933.3.
DR UCSC; uc004emu.4; human. [Q8TE76-1]
DR AGR; HGNC:23485; -.
DR CTD; 79710; -.
DR DisGeNET; 79710; -.
DR GeneCards; MORC4; -.
DR HGNC; HGNC:23485; MORC4.
DR HPA; ENSG00000133131; Tissue enhanced (placenta).
DR MIM; 300970; gene.
DR neXtProt; NX_Q8TE76; -.
DR OpenTargets; ENSG00000133131; -.
DR PharmGKB; PA128394718; -.
DR VEuPathDB; HostDB:ENSG00000133131; -.
DR eggNOG; KOG1845; Eukaryota.
DR GeneTree; ENSGT00940000161221; -.
DR HOGENOM; CLU_011516_3_0_1; -.
DR InParanoid; Q8TE76; -.
DR OMA; YKWIVGE; -.
DR OrthoDB; 933627at2759; -.
DR PhylomeDB; Q8TE76; -.
DR TreeFam; TF329118; -.
DR PathwayCommons; Q8TE76; -.
DR SignaLink; Q8TE76; -.
DR BioGRID-ORCS; 79710; 16 hits in 780 CRISPR screens.
DR ChiTaRS; MORC4; human.
DR GenomeRNAi; 79710; -.
DR Pharos; Q8TE76; Tbio.
DR PRO; PR:Q8TE76; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q8TE76; Protein.
DR Bgee; ENSG00000133131; Expressed in colonic epithelium and 173 other cell types or tissues.
DR ExpressionAtlas; Q8TE76; baseline and differential.
DR Genevisible; Q8TE76; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0035064; F:methylated histone binding; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR Gene3D; 3.30.40.100; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR045261; MORC_ATPase.
DR InterPro; IPR041006; Morc_S5.
DR InterPro; IPR011124; Znf_CW.
DR PANTHER; PTHR23336:SF22; MORC FAMILY CW-TYPE ZINC FINGER PROTEIN 4; 1.
DR PANTHER; PTHR23336; ZINC FINGER CW-TYPE COILED-COIL DOMAIN PROTEIN 3; 1.
DR Pfam; PF13589; HATPase_c_3; 1.
DR Pfam; PF17942; Morc6_S5; 1.
DR Pfam; PF07496; zf-CW; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR PROSITE; PS51050; ZF_CW; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Metal-binding; Nucleus;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..937
FT /note="MORC family CW-type zinc finger protein 4"
FT /id="PRO_0000096539"
FT ZN_FING 420..472
FT /note="CW-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00454"
FT REGION 606..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 762..876
FT /evidence="ECO:0000255"
FT BINDING 429
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00454"
FT BINDING 432
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00454"
FT BINDING 453
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00454"
FT BINDING 464
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00454"
FT VAR_SEQ 1..252
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17608765"
FT /id="VSP_045025"
FT VAR_SEQ 875..937
FT /note="VSYRTPEGDDLERALAKLTRLRIHVSYLLTSVLPHLELREIGYDSEQVDGIL
FT YTVLEANHILD -> GFGKAYAATYPRQLSPYFCPPSLGAS (in isoform 2 and
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:17608765"
FT /id="VSP_045026"
FT VARIANT 473
FT /note="T -> I (in dbSNP:rs6622126)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_051197"
FT VARIANT 653
FT /note="R -> C (in dbSNP:rs3827464)"
FT /id="VAR_051198"
FT CONFLICT 307
FT /note="Y -> H (in Ref. 3; BAB71125)"
FT /evidence="ECO:0000305"
FT CONFLICT 480
FT /note="S -> G (in Ref. 3; BAB13859)"
FT /evidence="ECO:0000305"
FT CONFLICT 519
FT /note="G -> E (in Ref. 1; ABL84747)"
FT /evidence="ECO:0000305"
FT HELIX 38..44
FT /evidence="ECO:0007829|PDB:7K7T"
FT HELIX 50..62
FT /evidence="ECO:0007829|PDB:7K7T"
FT TURN 64..66
FT /evidence="ECO:0007829|PDB:7K7T"
FT STRAND 69..77
FT /evidence="ECO:0007829|PDB:7K7T"
FT STRAND 79..88
FT /evidence="ECO:0007829|PDB:7K7T"
FT HELIX 95..101
FT /evidence="ECO:0007829|PDB:7K7T"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:7K7T"
FT HELIX 124..132
FT /evidence="ECO:0007829|PDB:7K7T"
FT STRAND 133..144
FT /evidence="ECO:0007829|PDB:7K7T"
FT STRAND 146..152
FT /evidence="ECO:0007829|PDB:7K7T"
FT HELIX 153..158
FT /evidence="ECO:0007829|PDB:7K7T"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:7K7T"
FT HELIX 185..194
FT /evidence="ECO:0007829|PDB:7K7T"
FT HELIX 200..205
FT /evidence="ECO:0007829|PDB:7K7T"
FT HELIX 206..209
FT /evidence="ECO:0007829|PDB:7K7T"
FT STRAND 210..223
FT /evidence="ECO:0007829|PDB:7K7T"
FT STRAND 229..237
FT /evidence="ECO:0007829|PDB:7K7T"
FT HELIX 263..265
FT /evidence="ECO:0007829|PDB:7K7T"
FT HELIX 268..274
FT /evidence="ECO:0007829|PDB:7K7T"
FT STRAND 275..278
FT /evidence="ECO:0007829|PDB:7K7T"
FT STRAND 281..285
FT /evidence="ECO:0007829|PDB:7K7T"
FT TURN 295..298
FT /evidence="ECO:0007829|PDB:7K7T"
FT STRAND 300..307
FT /evidence="ECO:0007829|PDB:7K7T"
FT STRAND 316..322
FT /evidence="ECO:0007829|PDB:7K7T"
FT STRAND 331..336
FT /evidence="ECO:0007829|PDB:7K7T"
FT STRAND 339..342
FT /evidence="ECO:0007829|PDB:7K7T"
FT STRAND 361..366
FT /evidence="ECO:0007829|PDB:7K7T"
FT STRAND 376..379
FT /evidence="ECO:0007829|PDB:7K7T"
FT HELIX 383..402
FT /evidence="ECO:0007829|PDB:7K7T"
FT STRAND 425..428
FT /evidence="ECO:0007829|PDB:7K7T"
FT TURN 430..432
FT /evidence="ECO:0007829|PDB:7K7T"
FT STRAND 435..440
FT /evidence="ECO:0007829|PDB:7K7T"
FT HELIX 453..455
FT /evidence="ECO:0007829|PDB:7K7T"
SQ SEQUENCE 937 AA; 106348 MW; 7AABDA01596475D2 CRC64;
MLLYRGAPAG PGAPGCGLAR PGGGPQAFGI RLSTMSPRYL QSNSSSHTRP FSAIAELLDN
AVDPDVSART VFIDVEEVKN KSCLTFTDDG CGMTPHKLHR MLSFGFTDKV IKKSQCPIGV
FGNGFKSGSM RLGKDALVFT KNGGTLTVGL LSQTYLECVQ AQAVIVPIVP FNQQNKKMII
TEDSLPSLEA ILNYSIFNRE NDLLAQFDAI PGKKGTRVLI WNIRRNKNGK SELDFDTDQY
DILVSDFDTE EKMTGGVTSE LPETEYSLRA FCGILYMKPR MKIFLRQKKV TTQMIAKSLA
NVEYDTYKPT FTNKQVRITF GFSCKNSNQF GIMMYHNNRL IKSFEKVGCQ VKPTRGEGVG
VIGVIECNFL KPAYNKQDFE YTKEYRLTIN ALAQKLNAYW KEKTSQDNFE TSTVARPIPK
VPDQTWVQCD ECLKWRKLPG KIDPSMLPAR WFCYYNSHPK YRRCSVPEEQ ELTDEDLCLS
KAKKQEQTVE EKKKMPMENE NHQVFSNPPK ILTVQEMAGL NNKTIGYEGI HSPSVLPSGG
EESRSPSLQL KPLDSSVLQF SSKYKWILGE EPVEKRRRLQ NEMTTPSLDY SMPAPYRRVE
APVAYPEGEN SHDKSSSERS TPPYLFPEYP EASKNTGQNR EVSILYPGAK DQRQGSLLPE
ELEDQMPRLV AEESNRGSTT INKEEVNKGP FVAVVGVAKG VRDSGAPIQL IPFNREELAE
RRKAVESWNP VPYSVASAAI PAAAIGEKAR GYEESEGHNT PKLKNQRELE ELKRTTEKLE
RVLAERNLFQ QKVEELEQER NHWQSEFKKV QHELVIYSTQ EAEGLYWSKK HMGYRQAEFQ
ILKAELERTK EEKQELKEKL KETETHLEML QKAQVSYRTP EGDDLERALA KLTRLRIHVS
YLLTSVLPHL ELREIGYDSE QVDGILYTVL EANHILD
//
