ZN532_HUMAN
ID ZN532_HUMAN Reviewed; 1301 AA.
AC Q9HCE3; Q4G0V6; Q7L7Z7; Q96QR7; Q9NVJ6;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Zinc finger protein 532;
GN Name=ZNF532; Synonyms=KIAA1629;
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].
RA Chen H., Wang N., DePaulo R.J. Jr., Ross C.A., McInnis M.G.;
RT "Identification of the full-length cDNA for a novel zinc finger gene on
RT human chromosome 18q21 as a candidate for bipolar disorder.";
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 681-1301.
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-205, AND IDENTIFICATION BY
RP 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-314, AND IDENTIFICATION BY
RP 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130; SER-133; SER-134;
RP SER-252; SER-307; SER-314; SER-434 AND SER-1140, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314 AND SER-1140, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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-459; LYS-516; LYS-980; LYS-1144
RP AND LYS-1167, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [11]
RP VARIANT [LARGE SCALE ANALYSIS] LEU-822.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: May be involved in transcriptional regulation.
CC -!- INTERACTION:
CC Q9HCE3; O00629: KPNA4; NbExp=2; IntAct=EBI-9691987, EBI-396343;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH36366.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAA91755.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB13455.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY039256; AAK72122.1; -; mRNA.
DR EMBL; AB046849; BAB13455.1; ALT_INIT; mRNA.
DR EMBL; BC036366; AAH36366.1; ALT_FRAME; mRNA.
DR EMBL; BC130618; AAI30619.1; -; mRNA.
DR EMBL; BC130620; AAI30621.1; -; mRNA.
DR EMBL; AK001559; BAA91755.1; ALT_INIT; mRNA.
DR CCDS; CCDS11969.1; -.
DR RefSeq; NP_001305655.1; NM_001318726.1.
DR RefSeq; NP_001305656.1; NM_001318727.1.
DR RefSeq; NP_001305657.1; NM_001318728.1.
DR RefSeq; NP_060651.2; NM_018181.5.
DR RefSeq; XP_016881301.1; XM_017025812.1.
DR RefSeq; XP_016881302.1; XM_017025813.1.
DR RefSeq; XP_016881303.1; XM_017025814.1.
DR RefSeq; XP_016881304.1; XM_017025815.1.
DR RefSeq; XP_016881305.1; XM_017025816.1.
DR RefSeq; XP_016881306.1; XM_017025817.1.
DR RefSeq; XP_016881307.1; XM_017025818.1.
DR AlphaFoldDB; Q9HCE3; -.
DR BioGRID; 120501; 10.
DR IntAct; Q9HCE3; 9.
DR MINT; Q9HCE3; -.
DR STRING; 9606.ENSP00000338217; -.
DR GlyGen; Q9HCE3; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q9HCE3; -.
DR PhosphoSitePlus; Q9HCE3; -.
DR BioMuta; ZNF532; -.
DR DMDM; 158564020; -.
DR EPD; Q9HCE3; -.
DR jPOST; Q9HCE3; -.
DR MassIVE; Q9HCE3; -.
DR MaxQB; Q9HCE3; -.
DR PaxDb; Q9HCE3; -.
DR PeptideAtlas; Q9HCE3; -.
DR PRIDE; Q9HCE3; -.
DR ProteomicsDB; 81686; -.
DR Antibodypedia; 9795; 47 antibodies from 11 providers.
DR DNASU; 55205; -.
DR Ensembl; ENST00000336078.8; ENSP00000338217.4; ENSG00000074657.14.
DR Ensembl; ENST00000589288.5; ENSP00000466007.1; ENSG00000074657.14.
DR Ensembl; ENST00000591083.5; ENSP00000468532.1; ENSG00000074657.14.
DR Ensembl; ENST00000591230.5; ENSP00000465709.1; ENSG00000074657.14.
DR Ensembl; ENST00000591808.6; ENSP00000468238.1; ENSG00000074657.14.
DR GeneID; 55205; -.
DR KEGG; hsa:55205; -.
DR MANE-Select; ENST00000591808.6; ENSP00000468238.1; NM_001375912.1; NP_001362841.1.
DR UCSC; uc002lho.4; human.
DR CTD; 55205; -.
DR DisGeNET; 55205; -.
DR GeneCards; ZNF532; -.
DR HGNC; HGNC:30940; ZNF532.
DR HPA; ENSG00000074657; Low tissue specificity.
DR MIM; 619066; gene.
DR neXtProt; NX_Q9HCE3; -.
DR OpenTargets; ENSG00000074657; -.
DR PharmGKB; PA134901858; -.
DR VEuPathDB; HostDB:ENSG00000074657; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000154437; -.
DR HOGENOM; CLU_006283_0_0_1; -.
DR InParanoid; Q9HCE3; -.
DR OMA; KQNAHAD; -.
DR OrthoDB; 180681at2759; -.
DR PhylomeDB; Q9HCE3; -.
DR TreeFam; TF329009; -.
DR PathwayCommons; Q9HCE3; -.
DR SignaLink; Q9HCE3; -.
DR BioGRID-ORCS; 55205; 18 hits in 1095 CRISPR screens.
DR ChiTaRS; ZNF532; human.
DR GenomeRNAi; 55205; -.
DR Pharos; Q9HCE3; Tdark.
DR PRO; PR:Q9HCE3; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; Q9HCE3; protein.
DR Bgee; ENSG00000074657; Expressed in ganglionic eminence and 200 other tissues.
DR ExpressionAtlas; Q9HCE3; baseline and differential.
DR Genevisible; Q9HCE3; HS.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR045914; Zn532-like.
DR InterPro; IPR041697; Znf-C2H2_11.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR47222; PTHR47222; 1.
DR Pfam; PF16622; zf-C2H2_11; 1.
DR SMART; SM00355; ZnF_C2H2; 15.
DR SUPFAM; SSF57667; SSF57667; 5.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 9.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 8.
PE 1: Evidence at protein level;
KW Acetylation; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..1301
FT /note="Zinc finger protein 532"
FT /id="PRO_0000299552"
FT ZN_FING 616..635
FT /note="C2H2-type 1; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 754..779
FT /note="C2H2-type 2; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 783..805
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 842..865
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 870..893
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 905..927
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 936..959
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1025..1048
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1055..1078
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1085..1111
FT /note="C2H2-type 10; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1203..1226
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1264..1286
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 26..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 281..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 983..1017
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1230..1263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..53
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..245
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..354
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 994..1013
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1246..1263
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 134
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 175
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q6NXK2"
FT MOD_RES 205
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 252
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 307
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 314
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 434
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 1140
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 459
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 516
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 980
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1144
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1167
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 761
FT /note="E -> D (in dbSNP:rs3737506)"
FT /id="VAR_034846"
FT VARIANT 822
FT /note="S -> L (in a breast cancer sample; somatic mutation;
FT dbSNP:rs771503724)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035585"
FT CONFLICT 972
FT /note="G -> S (in Ref. 3; AAH36366)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1301 AA; 141696 MW; 434E9519D144904A CRC64;
MTMGDMKTPD FDDLLAAFDI PDMVDPKAAI ESGHDDHESH MKQNAHGEDD SHAPSSSDVG
VSVIVKNVRN IDSSEGGEKD GHNPTGNGLH NGFLTASSLD SYSKDGAKSL KGDVPASEVT
LKDSTFSQFS PISSAEEFDD DEKIEVDDPP DKEDMRSSFR SNVLTGSAPQ QDYDKLKALG
GENSSKTGLS TSGNVEKNKA VKRETEASSI NLSVYEPFKV RKAEDKLKES SDKVLENRVL
DGKLSSEKND TSLPSVAPSK TKSSSKLSSC IAAIAALSAK KAASDSCKEP VANSRESSPL
PKEVNDSPRA ADKSPESQNL IDGTKKPSLK QPDSPRSISS ENSSKGSPSS PAGSTPAIPK
VRIKTIKTSS GEIKRTVTRV LPEVDLDSGK KPSEQTASVM ASVTSLLSSP ASAAVLSSPP
RAPLQSAVVT NAVSPAELTP KQVTIKPVAT AFLPVSAVKT AGSQVINLKL ANNTTVKATV
ISAASVQSAS SAIIKAANAI QQQTVVVPAS SLANAKLVPK TVHLANLNLL PQGAQATSEL
RQVLTKPQQQ IKQAIINAAA SQPPKKVSRV QVVSSLQSSV VEAFNKVLSS VNPVPVYIPN
LSPPANAGIT LPTRGYKCLE CGDSFALEKS LTQHYDRRSV RIEVTCNHCT KNLVFYNKCS
LLSHARGHKE KGVVMQCSHL ILKPVPADQM IVSPSSNTST STSTLQSPVG AGTHTVTKIQ
SGITGTVISA PSSTPITPAM PLDEDPSKLC RHSLKCLECN EVFQDETSLA THFQQAADTS
GQKTCTICQM LLPNQCSYAS HQRIHQHKSP YTCPECGAIC RSVHFQTHVT KNCLHYTRRV
GFRCVHCNVV YSDVAALKSH IQGSHCEVFY KCPICPMAFK SAPSTHSHAY TQHPGIKIGE
PKIIYKCSMC DTVFTLQTLL YRHFDQHIEN QKVSVFKCPD CSLLYAQKQL MMDHIKSMHG
TLKSIEGPPN LGINLPLSIK PATQNSANQN KEDTKSMNGK EKLEKKSPSP VKKSMETKKV
ASPGWTCWEC DCLFMQRDVY ISHVRKEHGK QMKKHPCRQC DKSFSSSHSL CRHNRIKHKG
IRKVYACSHC PDSRRTFTKR LMLEKHVQLM HGIKDPDLKE MTDATNEEET EIKEDTKVPS
PKRKLEEPVL EFRPPRGAIT QPLKKLKINV FKVHKCAVCG FTTENLLQFH EHIPQHKSDG
SSYQCRECGL CYTSHVSLSR HLFIVHKLKE PQPVSKQNGA GEDNQQENKP SHEDESPDGA
VSDRKCKVCA KTFETEAALN THMRTHGMAF IKSKRMSSAE K
