FWCH1_HUMAN
ID FWCH1_HUMAN Reviewed; 716 AA.
AC Q4VC44; D3DUA1; Q6ZSQ1; Q8WV62; Q9BQG6; Q9BUS5; Q9HCM0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=FLYWCH-type zinc finger-containing protein 1;
GN Name=FLYWCH1; Synonyms=KIAA1552;
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 [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=10997877; DOI=10.1093/dnares/7.4.271;
RA Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:273-281(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC TISSUE=Hippocampus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC TISSUE=Eye, Placenta, and Testis;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 273-716 (ISOFORM 3).
RC TISSUE=Amygdala;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 AND SER-696, 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-261; SER-503 AND
RP SER-591, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-371; SER-503 AND
RP SER-696, AND IDENTIFICATION BY 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 [10]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-393, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [11]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-134; LYS-393 AND LYS-685, 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).
RN [12]
RP STRUCTURE BY NMR OF 595-674.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the fifth FLYWCH domain of FLYWCH-type zinc finger-
RT containing protein 1.";
RL Submitted (AUG-2009) to the PDB data bank.
CC -!- INTERACTION:
CC Q4VC44; Q86Z20: CCDC125; NbExp=3; IntAct=EBI-719415, EBI-11977221;
CC Q4VC44; Q96IK5: GMCL1; NbExp=3; IntAct=EBI-719415, EBI-2548508;
CC Q4VC44; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-719415, EBI-5916454;
CC Q4VC44; Q96ED9-2: HOOK2; NbExp=3; IntAct=EBI-719415, EBI-10961706;
CC Q4VC44; O75031: HSF2BP; NbExp=3; IntAct=EBI-719415, EBI-7116203;
CC Q4VC44; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-719415, EBI-14069005;
CC Q4VC44; P50458: LHX2; NbExp=3; IntAct=EBI-719415, EBI-12179869;
CC Q4VC44; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-719415, EBI-11522433;
CC Q4VC44; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-719415, EBI-79165;
CC Q4VC44; Q96T49: PPP1R16B; NbExp=3; IntAct=EBI-719415, EBI-10293968;
CC Q4VC44; Q12933: TRAF2; NbExp=3; IntAct=EBI-719415, EBI-355744;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q4VC44-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q4VC44-2; Sequence=VSP_030279;
CC Name=3;
CC IsoId=Q4VC44-3; Sequence=VSP_030281;
CC Name=4;
CC IsoId=Q4VC44-4; Sequence=VSP_030278;
CC Name=5;
CC IsoId=Q4VC44-5; Sequence=VSP_030277, VSP_030280;
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB13378.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB046772; BAB13378.1; ALT_INIT; mRNA.
DR EMBL; AK127235; BAC86896.1; -; mRNA.
DR EMBL; CH471112; EAW85450.1; -; Genomic_DNA.
DR EMBL; CH471112; EAW85451.1; -; Genomic_DNA.
DR EMBL; BC001973; AAH01973.1; -; mRNA.
DR EMBL; BC018712; AAH18712.1; -; mRNA.
DR EMBL; BC028572; AAH28572.1; -; mRNA.
DR EMBL; AL136585; CAB66520.2; -; mRNA.
DR CCDS; CCDS45390.1; -. [Q4VC44-2]
DR CCDS; CCDS76809.1; -. [Q4VC44-1]
DR RefSeq; NP_001294997.1; NM_001308068.1. [Q4VC44-1]
DR RefSeq; NP_065963.1; NM_020912.1.
DR RefSeq; NP_115672.2; NM_032296.2. [Q4VC44-2]
DR RefSeq; XP_006721025.1; XM_006720962.3. [Q4VC44-3]
DR PDB; 2RPR; NMR; -; A=595-674.
DR PDBsum; 2RPR; -.
DR AlphaFoldDB; Q4VC44; -.
DR SMR; Q4VC44; -.
DR BioGRID; 123983; 32.
DR IntAct; Q4VC44; 25.
DR MINT; Q4VC44; -.
DR STRING; 9606.ENSP00000399938; -.
DR iPTMnet; Q4VC44; -.
DR PhosphoSitePlus; Q4VC44; -.
DR BioMuta; FLYWCH1; -.
DR DMDM; 166217021; -.
DR EPD; Q4VC44; -.
DR jPOST; Q4VC44; -.
DR MassIVE; Q4VC44; -.
DR MaxQB; Q4VC44; -.
DR PaxDb; Q4VC44; -.
DR PeptideAtlas; Q4VC44; -.
DR PRIDE; Q4VC44; -.
DR ProteomicsDB; 62302; -. [Q4VC44-1]
DR ProteomicsDB; 62303; -. [Q4VC44-2]
DR ProteomicsDB; 62304; -. [Q4VC44-3]
DR ProteomicsDB; 62305; -. [Q4VC44-4]
DR ProteomicsDB; 62306; -. [Q4VC44-5]
DR Antibodypedia; 23928; 57 antibodies from 15 providers.
DR DNASU; 84256; -.
DR Ensembl; ENST00000253928.14; ENSP00000253928.9; ENSG00000059122.17. [Q4VC44-1]
DR Ensembl; ENST00000416288.6; ENSP00000399938.2; ENSG00000059122.17. [Q4VC44-2]
DR GeneID; 84256; -.
DR KEGG; hsa:84256; -.
DR MANE-Select; ENST00000253928.14; ENSP00000253928.9; NM_001308068.2; NP_001294997.1.
DR UCSC; uc002csc.4; human. [Q4VC44-1]
DR CTD; 84256; -.
DR DisGeNET; 84256; -.
DR GeneCards; FLYWCH1; -.
DR HGNC; HGNC:25404; FLYWCH1.
DR HPA; ENSG00000059122; Low tissue specificity.
DR neXtProt; NX_Q4VC44; -.
DR OpenTargets; ENSG00000059122; -.
DR PharmGKB; PA142671760; -.
DR VEuPathDB; HostDB:ENSG00000059122; -.
DR eggNOG; ENOG502SQTE; Eukaryota.
DR GeneTree; ENSGT00530000064166; -.
DR HOGENOM; CLU_023177_0_0_1; -.
DR InParanoid; Q4VC44; -.
DR OMA; LAQWEGP; -.
DR PhylomeDB; Q4VC44; -.
DR TreeFam; TF337169; -.
DR PathwayCommons; Q4VC44; -.
DR SignaLink; Q4VC44; -.
DR BioGRID-ORCS; 84256; 23 hits in 1080 CRISPR screens.
DR ChiTaRS; FLYWCH1; human.
DR EvolutionaryTrace; Q4VC44; -.
DR GenomeRNAi; 84256; -.
DR Pharos; Q4VC44; Tdark.
DR PRO; PR:Q4VC44; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q4VC44; protein.
DR Bgee; ENSG00000059122; Expressed in right hemisphere of cerebellum and 174 other tissues.
DR ExpressionAtlas; Q4VC44; baseline and differential.
DR Genevisible; Q4VC44; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR029279; FLYWCH_N.
DR InterPro; IPR040312; FWCH1/FWCH2.
DR InterPro; IPR007588; Znf_FLYWCH.
DR PANTHER; PTHR31665; PTHR31665; 1.
DR Pfam; PF04500; FLYWCH; 5.
DR Pfam; PF15423; FLYWCH_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; DNA-binding; Isopeptide bond;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..716
FT /note="FLYWCH-type zinc finger-containing protein 1"
FT /id="PRO_0000314460"
FT ZN_FING 116..174
FT /note="FLYWCH-type 1"
FT ZN_FING 273..331
FT /note="FLYWCH-type 2"
FT ZN_FING 421..479
FT /note="FLYWCH-type 3"
FT ZN_FING 509..567
FT /note="FLYWCH-type 4"
FT ZN_FING 600..658
FT /note="FLYWCH-type 5"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 191..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..416
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 261
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 371
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 503
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 591
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 696
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 134
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 393
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 685
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..388
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_030277"
FT VAR_SEQ 1..325
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030278"
FT VAR_SEQ 108
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10997877"
FT /id="VSP_030279"
FT VAR_SEQ 389..504
FT /note="RKRAKVEDQELPTQPEAPDEHQDMDADPGGPEFLKTPLGGSFLVYESFLYRR
FT EKAAGEKVYWTCRDQARMGCRSRAITQGRRVTVMRGHCHPPDLGGLEALRQREKRPNTA
FT QRGSP -> MPQATSPPLWPLSLHGGKGILWARHSHPPGPPSHHIQDSGRCSLPLPQSP
FT GVTPLPARLSGATPLSPIRLLSSFVPRGPRVIPLTNQARRTLHASLGGCWGRTSDAADT
FT ASLKAWQ (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_030280"
FT VAR_SEQ 504
FT /note="P -> PGAGLSFQWLFRILQLLGHAPVLLCPSGSSCLPSLPAPHGPCPALSI
FT PLE (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11230166"
FT /id="VSP_030281"
FT CONFLICT 666
FT /note="E -> G (in Ref. 4; AAH28572)"
FT /evidence="ECO:0000305"
FT STRAND 599..603
FT /evidence="ECO:0007829|PDB:2RPR"
FT TURN 604..606
FT /evidence="ECO:0007829|PDB:2RPR"
FT STRAND 607..612
FT /evidence="ECO:0007829|PDB:2RPR"
FT STRAND 615..622
FT /evidence="ECO:0007829|PDB:2RPR"
FT STRAND 627..631
FT /evidence="ECO:0007829|PDB:2RPR"
FT HELIX 632..634
FT /evidence="ECO:0007829|PDB:2RPR"
FT STRAND 642..646
FT /evidence="ECO:0007829|PDB:2RPR"
FT STRAND 649..652
FT /evidence="ECO:0007829|PDB:2RPR"
FT HELIX 662..670
FT /evidence="ECO:0007829|PDB:2RPR"
SQ SEQUENCE 716 AA; 80108 MW; BC1DD372CA925A72 CRC64;
MPLPEPSEQE GESVKAGQEP SPKPGTDVIP AAPRKPREFS KLVLLTASDQ DEDGVGSKPQ
EVHCVLSLEM AGPATLASTL QILPVEEQGG VVQPALEMPE QKCSKLDAAA PQSLEFLRTP
FGGRLLVLES FLYKQEKAVG DKVYWKCRQH AELGCRGRAI TRGLRATVMR GHCHAPDEQG
LEARRQREKL PSLALPEGLG EPQGPEGPGG RVEEPLEGVG PWQCPEEPEP TPGLVLSKPA
LEEEEAPRAL SLLSLPPKKR SILGLGQARP LEFLRTCYGG SFLVHESFLY KREKAVGDKV
YWTCRDHALH GCRSRAITQG QRVTVMRGHC HQPDMEGLEA RRQQEKAVET LQAGQDGPGS
QVDTLLRGVD SLLYRRGPGP LTLTRPRPRK RAKVEDQELP TQPEAPDEHQ DMDADPGGPE
FLKTPLGGSF LVYESFLYRR EKAAGEKVYW TCRDQARMGC RSRAITQGRR VTVMRGHCHP
PDLGGLEALR QREKRPNTAQ RGSPGGPEFL KTPLGGSFLV YESFLYRREK AAGEKVYWTC
RDQARMGCRS RAITQGRRVM VMRRHCHPPD LGGLEALRQR EHFPNLAQWD SPDPLRPLEF
LRTSLGGRFL VHESFLYRKE KAAGEKVYWM CRDQARLGCR SRAITQGHRI MVMRSHCHQP
DLAGLEALRQ RERLPTTAQQ EDPEKIQVQL CFKTCSPESQ QIYGDIKDVR LDGESQ
