ZN460_HUMAN
ID ZN460_HUMAN Reviewed; 562 AA.
AC Q14592; A4FU64; B4DNX9; Q2VPC7; Q6VSF8;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Zinc finger protein 460;
DE AltName: Full=Zinc finger protein 272;
DE AltName: Full=Zinc finger protein HZF8;
GN Name=ZNF460; Synonyms=ZNF272;
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), AND TISSUE SPECIFICITY.
RC TISSUE=Fetal brain;
RX PubMed=15004467; DOI=10.1159/000076292;
RA Dai J., Li Y., Ji C., Jin F., Zheng Z., Wang X., Sun X., Xu X., Gu S.,
RA Xie Y., Mao Y.;
RT "Characterization of two novel KRAB-domain-containing zinc finger genes,
RT ZNF460 and ZNF461, on human chromosome 19q13.1-q13.4.";
RL Cytogenet. Genome Res. 103:74-78(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Lung;
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].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [MRNA] OF 389-562 (ISOFORM 1).
RX PubMed=7865130; DOI=10.1089/dna.1995.14.125;
RA Abrink M., Aveskogh M., Hellman L.;
RT "Isolation of cDNA clones for 42 different Kruppel-related zinc finger
RT proteins expressed in the human monoblast cell line U-937.";
RL DNA Cell Biol. 14:125-136(1995).
RN [6]
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 SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-194; LYS-209; LYS-278; LYS-306
RP AND LYS-362, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [8]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-362, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [9]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-278; LYS-306 AND LYS-362, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [10]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-117; LYS-194; LYS-203; LYS-207;
RP LYS-209; LYS-250; LYS-278; LYS-287; LYS-300; LYS-305; LYS-306; LYS-362;
RP LYS-371; LYS-446 AND LYS-455, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 be involved in transcriptional regulation.
CC -!- INTERACTION:
CC Q14592; Q05D60: DEUP1; NbExp=3; IntAct=EBI-2555738, EBI-748597;
CC Q14592; G5E9A7: DMWD; NbExp=3; IntAct=EBI-2555738, EBI-10976677;
CC Q14592; P61328: FGF12; NbExp=3; IntAct=EBI-2555738, EBI-6657662;
CC Q14592; P25800: LMO1; NbExp=3; IntAct=EBI-2555738, EBI-8639312;
CC Q14592; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-2555738, EBI-5235340;
CC Q14592; Q8WV44: TRIM41; NbExp=3; IntAct=EBI-2555738, EBI-725997;
CC Q14592; P15622-3: ZNF250; NbExp=3; IntAct=EBI-2555738, EBI-10177272;
CC Q14592; Q9Y3S2: ZNF330; NbExp=3; IntAct=EBI-2555738, EBI-373456;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q14592-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q14592-2; Sequence=VSP_055954;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed at low levels. Highest
CC levels are found in pancreas and liver. {ECO:0000269|PubMed:15004467}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AY329492; AAR00225.1; -; mRNA.
DR EMBL; AK298106; BAG60391.1; -; mRNA.
DR EMBL; AC005261; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC109018; AAI09019.1; -; mRNA.
DR EMBL; BC109019; AAI09020.1; -; mRNA.
DR EMBL; BC118625; AAI18626.1; -; mRNA.
DR EMBL; X78931; CAA55531.1; -; mRNA.
DR CCDS; CCDS12949.1; -. [Q14592-1]
DR CCDS; CCDS82404.1; -. [Q14592-2]
DR PIR; S47069; S47069.
DR RefSeq; NP_001317551.1; NM_001330622.1. [Q14592-2]
DR RefSeq; NP_006626.3; NM_006635.3. [Q14592-1]
DR AlphaFoldDB; Q14592; -.
DR SMR; Q14592; -.
DR BioGRID; 116009; 139.
DR IntAct; Q14592; 34.
DR STRING; 9606.ENSP00000353491; -.
DR iPTMnet; Q14592; -.
DR PhosphoSitePlus; Q14592; -.
DR SwissPalm; Q14592; -.
DR BioMuta; ZNF460; -.
DR DMDM; 85681860; -.
DR EPD; Q14592; -.
DR jPOST; Q14592; -.
DR MassIVE; Q14592; -.
DR MaxQB; Q14592; -.
DR PaxDb; Q14592; -.
DR PeptideAtlas; Q14592; -.
DR PRIDE; Q14592; -.
DR ProteomicsDB; 4735; -.
DR ProteomicsDB; 60067; -. [Q14592-1]
DR Antibodypedia; 33241; 110 antibodies from 25 providers.
DR DNASU; 10794; -.
DR Ensembl; ENST00000360338.4; ENSP00000353491.2; ENSG00000197714.9. [Q14592-1]
DR Ensembl; ENST00000537645.5; ENSP00000446167.1; ENSG00000197714.9. [Q14592-2]
DR GeneID; 10794; -.
DR KEGG; hsa:10794; -.
DR MANE-Select; ENST00000360338.4; ENSP00000353491.2; NM_006635.4; NP_006626.3.
DR UCSC; uc002qog.3; human. [Q14592-1]
DR CTD; 10794; -.
DR DisGeNET; 10794; -.
DR GeneCards; ZNF460; -.
DR HGNC; HGNC:21628; ZNF460.
DR HPA; ENSG00000197714; Tissue enriched (brain).
DR MIM; 604755; gene.
DR neXtProt; NX_Q14592; -.
DR OpenTargets; ENSG00000197714; -.
DR PharmGKB; PA37642; -.
DR VEuPathDB; HostDB:ENSG00000197714; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00950000182890; -.
DR HOGENOM; CLU_002678_5_1_1; -.
DR InParanoid; Q14592; -.
DR OMA; QHEQIHI; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q14592; -.
DR TreeFam; TF340405; -.
DR PathwayCommons; Q14592; -.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR SignaLink; Q14592; -.
DR BioGRID-ORCS; 10794; 12 hits in 1098 CRISPR screens.
DR GenomeRNAi; 10794; -.
DR Pharos; Q14592; Tdark.
DR PRO; PR:Q14592; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q14592; protein.
DR Bgee; ENSG00000197714; Expressed in adrenal tissue and 111 other tissues.
DR ExpressionAtlas; Q14592; baseline and differential.
DR Genevisible; Q14592; HS.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
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; 11.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 7.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 11.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 11.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..562
FT /note="Zinc finger protein 460"
FT /id="PRO_0000047499"
FT DOMAIN 13..99
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 196..218
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 224..246
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 252..274
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 280..302
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 308..330
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 336..358
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 364..386
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 392..414
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 420..442
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 448..470
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 476..498
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT CROSSLNK 117
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 194
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 203
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 207
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 209
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 250
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 278
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733"
FT CROSSLNK 287
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 300
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 305
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 306
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733"
FT CROSSLNK 362
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 371
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 446
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 455
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..41
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055954"
FT CONFLICT 451
FT /note="I -> T (in Ref. 1; AAR00225)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 562 AA; 63665 MW; D74C8AA7DC4ECC79 CRC64;
MAAAWMAPAQ ESVTFEDVAV TFTQEEWGQL DVTQRALYVE VMLETCGLLV ALGDSTKPET
VEPIPSHLAL PEEVSLQEQL AQGVPRYSYL GQAMDQDGPS EMQEYFLRPG TDPQSEKLHG
KMSLEHEGLA TADGICSMMI QNQVSPEDAL YGFDSYGPVT DSLIHEGENS YKFEEMFNEN
CFLVQHEQIL PRVKPYDCPE CGKAFGKSKH LLQHHIIHTG EKPYKCLECG KDFNRRSHLT
RHQRTHNGDK PFVCSECGRT FNRGSHLTRH QRVHSGEKPF VCNECGKAFT YRSNFVLHNK
SHNEKKPFAC SECGKGFYES TALIQHFIIH TGERPFKCLE CGKAFNCRSH LKQHERIHTG
EKPFVCSQCG KAFTHYSTYV LHERAHTGEK PFECKECGKA FSIRKDLIRH FNIHTGEKPY
ECLQCGKAFT RMSGLTRHQW IHTGEKPYVC IQCGKAFCRT TNLIRHFSIH TGEKPYECVE
CGKAFNRRSP LTRHQRIHTA EKSHEPIQSG NVSCESTDLI QHSIIHTESS PVSAVNMETP
SIAAHSSSLD INGFIVEETL PL
