ZSC31_HUMAN
ID ZSC31_HUMAN Reviewed; 406 AA.
AC Q96LW9; Q6P178; Q8WWS5;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2002, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Zinc finger and SCAN domain-containing protein 31;
DE AltName: Full=Zinc finger protein 323;
GN Name=ZSCAN31; Synonyms=ZNF310P, ZNF323;
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 heart;
RX PubMed=12147252; DOI=10.1016/s0006-291x(02)00772-6;
RA Pi H., Li Y., Zhu C., Zhou L., Luo K., Yuan W., Yi Z., Wang Y., Wu X.,
RA Liu M.;
RT "A novel human SCAN/(Cys)2(His)2 zinc-finger transcription factor ZNF323 in
RT early human embryonic development.";
RL Biochem. Biophys. Res. Commun. 296:206-213(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Uterus;
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=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=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 [6]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-14 AND LYS-149, AND
RP IDENTIFICATION BY MASS 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 [7]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-14 AND LYS-149, AND
RP IDENTIFICATION BY MASS 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 [8]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-14 AND LYS-149, 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 [9]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-14; LYS-149; LYS-191; LYS-205;
RP LYS-215; LYS-250 AND LYS-358, 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 function as a transcription factor. May be involved in
CC the development of multiple embryonic organs.
CC -!- INTERACTION:
CC Q96LW9-2; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-25932549, EBI-5235340;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96LW9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96LW9-2; Sequence=VSP_047105;
CC -!- TISSUE SPECIFICITY: Expressed at high levels in the lung, liver, and
CC kidney, while weakly expressed in intestine, brain, muscle, cholecyst,
CC heart, and pancreas. {ECO:0000269|PubMed:12147252}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AF513019; AAM47006.1; -; mRNA.
DR EMBL; AK057702; BAB71548.1; -; mRNA.
DR EMBL; AL021997; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471081; EAX03155.1; -; Genomic_DNA.
DR EMBL; BC065241; AAH65241.1; -; mRNA.
DR CCDS; CCDS4649.1; -. [Q96LW9-1]
DR CCDS; CCDS59001.1; -. [Q96LW9-2]
DR RefSeq; NP_001128687.1; NM_001135215.1. [Q96LW9-1]
DR RefSeq; NP_001128688.1; NM_001135216.1. [Q96LW9-1]
DR RefSeq; NP_001230170.1; NM_001243241.1. [Q96LW9-1]
DR RefSeq; NP_001230171.1; NM_001243242.1. [Q96LW9-2]
DR RefSeq; NP_001230172.1; NM_001243243.1. [Q96LW9-2]
DR RefSeq; NP_001230173.1; NM_001243244.1. [Q96LW9-2]
DR RefSeq; NP_112161.3; NM_030899.4. [Q96LW9-1]
DR RefSeq; NP_665916.1; NM_145909.2. [Q96LW9-1]
DR RefSeq; XP_005249352.1; XM_005249295.1. [Q96LW9-1]
DR RefSeq; XP_005249353.1; XM_005249296.4. [Q96LW9-1]
DR RefSeq; XP_011513109.1; XM_011514807.2. [Q96LW9-1]
DR RefSeq; XP_011513110.1; XM_011514808.2. [Q96LW9-1]
DR RefSeq; XP_011513111.1; XM_011514809.1. [Q96LW9-1]
DR RefSeq; XP_011513113.1; XM_011514811.2. [Q96LW9-1]
DR RefSeq; XP_011513114.1; XM_011514812.2. [Q96LW9-1]
DR RefSeq; XP_011513115.1; XM_011514813.2. [Q96LW9-1]
DR RefSeq; XP_016866685.1; XM_017011196.1. [Q96LW9-1]
DR AlphaFoldDB; Q96LW9; -.
DR SMR; Q96LW9; -.
DR BioGRID; 122130; 18.
DR IntAct; Q96LW9; 13.
DR STRING; 9606.ENSP00000390076; -.
DR iPTMnet; Q96LW9; -.
DR PhosphoSitePlus; Q96LW9; -.
DR BioMuta; ZSCAN31; -.
DR DMDM; 23396994; -.
DR EPD; Q96LW9; -.
DR jPOST; Q96LW9; -.
DR MassIVE; Q96LW9; -.
DR MaxQB; Q96LW9; -.
DR PaxDb; Q96LW9; -.
DR PeptideAtlas; Q96LW9; -.
DR PRIDE; Q96LW9; -.
DR ProteomicsDB; 66823; -.
DR ProteomicsDB; 77261; -. [Q96LW9-1]
DR ABCD; Q96LW9; 5 sequenced antibodies.
DR Antibodypedia; 25874; 139 antibodies from 25 providers.
DR DNASU; 64288; -.
DR Ensembl; ENST00000344279.11; ENSP00000345339.6; ENSG00000235109.8. [Q96LW9-1]
DR Ensembl; ENST00000396838.6; ENSP00000380050.2; ENSG00000235109.8. [Q96LW9-1]
DR Ensembl; ENST00000414429.5; ENSP00000390076.1; ENSG00000235109.8. [Q96LW9-1]
DR Ensembl; ENST00000439158.5; ENSP00000413705.1; ENSG00000235109.8. [Q96LW9-1]
DR Ensembl; ENST00000446474.5; ENSP00000402937.1; ENSG00000235109.8. [Q96LW9-2]
DR Ensembl; ENST00000611469.4; ENSP00000480254.1; ENSG00000235109.8. [Q96LW9-2]
DR GeneID; 64288; -.
DR KEGG; hsa:64288; -.
DR MANE-Select; ENST00000344279.11; ENSP00000345339.6; NM_030899.5; NP_112161.3.
DR UCSC; uc003nla.4; human. [Q96LW9-1]
DR CTD; 64288; -.
DR DisGeNET; 64288; -.
DR GeneCards; ZSCAN31; -.
DR HGNC; HGNC:14097; ZSCAN31.
DR HPA; ENSG00000235109; Tissue enhanced (brain).
DR MIM; 610794; gene.
DR neXtProt; NX_Q96LW9; -.
DR OpenTargets; ENSG00000235109; -.
DR PharmGKB; PA37840; -.
DR VEuPathDB; HostDB:ENSG00000235109; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000163314; -.
DR HOGENOM; CLU_002678_49_3_1; -.
DR InParanoid; Q96LW9; -.
DR OMA; QWLRPDT; -.
DR PhylomeDB; Q96LW9; -.
DR TreeFam; TF338304; -.
DR PathwayCommons; Q96LW9; -.
DR SignaLink; Q96LW9; -.
DR BioGRID-ORCS; 64288; 16 hits in 1087 CRISPR screens.
DR ChiTaRS; ZSCAN31; human.
DR GenomeRNAi; 64288; -.
DR Pharos; Q96LW9; Tdark.
DR PRO; PR:Q96LW9; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q96LW9; protein.
DR Bgee; ENSG00000235109; Expressed in left testis and 164 other tissues.
DR ExpressionAtlas; Q96LW9; baseline and differential.
DR Genevisible; Q96LW9; 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:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd07936; SCAN; 1.
DR Gene3D; 1.10.4020.10; -; 1.
DR InterPro; IPR003309; SCAN_dom.
DR InterPro; IPR038269; SCAN_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF02023; SCAN; 1.
DR Pfam; PF00096; zf-C2H2; 5.
DR SMART; SM00431; SCAN; 1.
DR SMART; SM00355; ZnF_C2H2; 6.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS50804; SCAN_BOX; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6.
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..406
FT /note="Zinc finger and SCAN domain-containing protein 31"
FT /id="PRO_0000047532"
FT DOMAIN 39..121
FT /note="SCAN box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00187"
FT ZN_FING 239..261
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 267..289
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 295..317
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 323..345
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 351..373
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 379..401
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT CROSSLNK 14
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 149
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 191
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 205
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 215
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="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 358
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..159
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_047105"
FT VARIANT 50
FT /note="T -> S (in dbSNP:rs853678)"
FT /id="VAR_019981"
FT VARIANT 128
FT /note="A -> P (in dbSNP:rs6922302)"
FT /id="VAR_052809"
FT VARIANT 205
FT /note="K -> R (in dbSNP:rs853684)"
FT /id="VAR_024209"
FT VARIANT 222
FT /note="R -> Q (in dbSNP:rs34223404)"
FT /id="VAR_052810"
FT VARIANT 365
FT /note="G -> E (in dbSNP:rs2394051)"
FT /id="VAR_059911"
FT CONFLICT 58
FT /note="S -> N (in Ref. 2; BAB71548)"
FT /evidence="ECO:0000305"
FT CONFLICT 173
FT /note="Q -> R (in Ref. 2; BAB71548)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 406 AA; 47293 MW; A6082E44F27101E8 CRC64;
MASTEEQYDL KIVKVEEDPI WDQETHLRGN NFSGQEASRQ LFRQFCYQET PGPREALSRL
RELCHQWLRP EIHTKEQILE LLVLEQFLTI LPEELQAWVR EHHPESGEEA VAVVEDLEQE
LSEPGNQAPD HEHGHSEVLL EDVEHLKVKQ EPTDIQLQPM VTQLRYESFC LHQFQEQDGE
SIPENQELAS KQEILKEMEH LGDSKLQRDV SLDSKYRETC KRDSKAEKQQ AHSTGERRHR
CNECGKSFTK SSVLIEHQRI HTGEKPYECE ECGKAFSRRS SLNEHRRSHT GEKPYQCKEC
GKAFSASNGL TRHRRIHTGE KPYECKVCGK AFLLSSCLVQ HQRIHTGEKR YQCRECGKAF
IQNAGLFQHL RVHTGEKPYQ CSQCSKLFSK RTLLKKHQKI HTGERP
