SALL2_HUMAN
ID SALL2_HUMAN Reviewed; 1007 AA.
AC Q9Y467; B2RMX6; B9EGK8; Q8N656; Q9Y4G1;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 4.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Sal-like protein 2;
DE AltName: Full=Zinc finger protein 795;
DE AltName: Full=Zinc finger protein SALL2;
DE AltName: Full=Zinc finger protein Spalt-2;
DE Short=Sal-2;
DE Short=hSal2;
GN Name=SALL2; Synonyms=KIAA0360, SAL2, ZNF795;
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 VARIANTS SER-122 AND ARG-746.
RC TISSUE=Fetus;
RX PubMed=8975705; DOI=10.1006/geno.1996.0631;
RA Kohlhase J., Schuh R., Dowe G., Kuehnlein R.P., Jaeckle H., Schroeder B.,
RA Schulz-Schaeffer W., Kretzschmar H.A., Koehler A., Mueller U.,
RA Raab-Vetter M., Burkhardt E., Engel W., Stick R.;
RT "Isolation, characterization, and organ-specific expression of two novel
RT human zinc finger genes related to the Drosophila gene spalt.";
RL Genomics 38:291-298(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS SER-122
RP AND ARG-746.
RC TISSUE=Brain;
RX PubMed=9205841; DOI=10.1093/dnares/4.2.141;
RA Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VII. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 4:141-150(1997).
RN [3]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP SER-122.
RC TISSUE=Brain;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 541-1005 (ISOFORM 1), AND VARIANT ARG-746.
RA Morgan J.W., Ford D., Ma Y., Maizel A.L.;
RT "Homo sapiens mRNA for zinc finger protein, SALL2 exon 2.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP DOMAIN.
RX PubMed=16545361; DOI=10.1016/j.ydbio.2006.02.009;
RA Sweetman D., Muensterberg A.;
RT "The vertebrate spalt genes in development and disease.";
RL Dev. Biol. 293:285-293(2006).
RN [8]
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 [9]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-911, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=18655026; DOI=10.1002/pmic.200700887;
RA Tan F., Lu L., Cai Y., Wang J., Xie Y., Wang L., Gong Y., Xu B.-E., Wu J.,
RA Luo Y., Qiang B., Yuan J., Sun X., Peng X.;
RT "Proteomic analysis of ubiquitinated proteins in normal hepatocyte cell
RT line Chang liver cells.";
RL Proteomics 8:2885-2896(2008).
RN [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-797; SER-802 AND SER-806, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243; SER-802 AND SER-806, AND
RP IDENTIFICATION BY MASS 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 [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [14]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INVOLVEMENT IN COAR.
RX PubMed=24412933; DOI=10.1093/hmg/ddt643;
RA Kelberman D., Islam L., Lakowski J., Bacchelli C., Chanudet E., Lescai F.,
RA Patel A., Stupka E., Buck A., Wolf S., Beales P.L., Jacques T.S.,
RA Bitner-Glindzicz M., Liasis A., Lehmann O.J., Kohlhase J., Nischal K.K.,
RA Sowden J.C.;
RT "Mutation of SALL2 causes recessive ocular coloboma in humans and mice.";
RL Hum. Mol. Genet. 23:2511-2526(2014).
CC -!- FUNCTION: Probable transcription factor that plays a role in eye
CC development before, during, and after optic fissure closure.
CC {ECO:0000269|PubMed:24412933}.
CC -!- INTERACTION:
CC Q9Y467; Q8TAP6: CEP76; NbExp=4; IntAct=EBI-746180, EBI-742887;
CC Q9Y467; P08138: NGFR; NbExp=3; IntAct=EBI-746180, EBI-1387782;
CC Q9Y467; Q8NF64-2: ZMIZ2; NbExp=3; IntAct=EBI-746180, EBI-10182121;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y467-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y467-3; Sequence=VSP_056251, VSP_056252, VSP_056253;
CC -!- TISSUE SPECIFICITY: Highest levels in adult brain (in different areas).
CC Lower levels in heart; very low levels in kidney and pancreas.
CC Expressed throughout the retina and lens vesicle as well as the
CC periocular mesenchyme. {ECO:0000269|PubMed:24412933}.
CC -!- DEVELOPMENTAL STAGE: In fetal brain exclusively in pontine nuclei.
CC Expressed at 5 weeks of development, the stage at which optic fissure
CC closure starts. Expression is maintained in the developing retina up to
CC 8 weeks; after completion of fissure closure, it is restricted to the
CC inner neuroblastic layer. Expressed in the cornea, lens, and retina at
CC different developmental stages. {ECO:0000269|PubMed:24412933}.
CC -!- DISEASE: Coloboma, ocular, autosomal recessive (COAR) [MIM:216820]: An
CC ocular anomaly resulting from abnormal morphogenesis of the optic cup
CC and stalk, and incomplete fusion of the fetal intra-ocular fissure
CC during gestation. The clinical presentation is variable. Some
CC individuals may present with minimal defects in the anterior iris leaf
CC without other ocular defects. More complex malformations create a
CC combination of iris, uveoretinal and/or optic nerve defects without or
CC with microphthalmia or even anophthalmia.
CC {ECO:0000269|PubMed:24412933}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the sal C2H2-type zinc-finger protein family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA21638.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X98834; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AB002358; BAA21638.2; ALT_INIT; mRNA.
DR EMBL; AE000521; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AE000658; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC024245; AAH24245.1; -; mRNA.
DR EMBL; BC090958; AAH90958.1; -; mRNA.
DR EMBL; BC136528; AAI36529.1; -; mRNA.
DR EMBL; BC136529; AAI36530.1; -; mRNA.
DR EMBL; AF465630; AAL74188.1; -; mRNA.
DR CCDS; CCDS32045.1; -. [Q9Y467-1]
DR RefSeq; NP_001278375.1; NM_001291446.1.
DR RefSeq; NP_001278376.1; NM_001291447.1.
DR RefSeq; NP_005398.2; NM_005407.2.
DR AlphaFoldDB; Q9Y467; -.
DR BioGRID; 112204; 74.
DR IntAct; Q9Y467; 29.
DR MINT; Q9Y467; -.
DR STRING; 9606.ENSP00000483562; -.
DR GlyGen; Q9Y467; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q9Y467; -.
DR PhosphoSitePlus; Q9Y467; -.
DR BioMuta; SALL2; -.
DR DMDM; 296453020; -.
DR EPD; Q9Y467; -.
DR jPOST; Q9Y467; -.
DR MassIVE; Q9Y467; -.
DR MaxQB; Q9Y467; -.
DR PaxDb; Q9Y467; -.
DR PeptideAtlas; Q9Y467; -.
DR PRIDE; Q9Y467; -.
DR ProteomicsDB; 72132; -.
DR ProteomicsDB; 86114; -. [Q9Y467-1]
DR Antibodypedia; 22191; 100 antibodies from 20 providers.
DR DNASU; 6297; -.
DR Ensembl; ENST00000614342.1; ENSP00000483562.1; ENSG00000165821.12.
DR GeneID; 6297; -.
DR KEGG; hsa:6297; -.
DR UCSC; uc032atc.2; human. [Q9Y467-1]
DR CTD; 6297; -.
DR DisGeNET; 6297; -.
DR GeneCards; SALL2; -.
DR HGNC; HGNC:10526; SALL2.
DR HPA; ENSG00000165821; Tissue enhanced (brain).
DR MalaCards; SALL2; -.
DR MIM; 216820; phenotype.
DR MIM; 602219; gene.
DR neXtProt; NX_Q9Y467; -.
DR Orphanet; 98942; Coloboma of choroid and retina.
DR Orphanet; 98943; Coloboma of eye lens.
DR Orphanet; 98946; Coloboma of eyelid.
DR Orphanet; 98944; Coloboma of iris.
DR Orphanet; 98945; Coloboma of macula.
DR Orphanet; 98947; Coloboma of optic disc.
DR Orphanet; 99861; Precursor T-cell acute lymphoblastic leukemia.
DR PharmGKB; PA34934; -.
DR VEuPathDB; HostDB:ENSG00000165821; -.
DR eggNOG; KOG1074; Eukaryota.
DR HOGENOM; CLU_013111_0_0_1; -.
DR InParanoid; Q9Y467; -.
DR OrthoDB; 244207at2759; -.
DR PhylomeDB; Q9Y467; -.
DR TreeFam; TF317003; -.
DR PathwayCommons; Q9Y467; -.
DR SignaLink; Q9Y467; -.
DR SIGNOR; Q9Y467; -.
DR BioGRID-ORCS; 6297; 12 hits in 1097 CRISPR screens.
DR ChiTaRS; SALL2; human.
DR GeneWiki; SALL2; -.
DR GenomeRNAi; 6297; -.
DR Pharos; Q9Y467; Tbio.
DR PRO; PR:Q9Y467; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q9Y467; protein.
DR Bgee; ENSG00000165821; Expressed in cerebellar vermis and 175 other tissues.
DR ExpressionAtlas; Q9Y467; baseline and differential.
DR Genevisible; Q9Y467; HS.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
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:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0001654; P:eye development; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:NTNU_SB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 3.
DR SMART; SM00355; ZnF_C2H2; 7.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 7.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 7.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..1007
FT /note="Sal-like protein 2"
FT /id="PRO_0000047022"
FT ZN_FING 34..56
FT /note="C2H2-type 1; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042,
FT ECO:0000303|PubMed:16545361"
FT ZN_FING 373..395
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 401..423
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 631..653
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 659..681
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 691..713
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 911..933
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 940..963
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 59..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 220..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 286..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 520..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 610..629
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 714..886
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..174
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 733..758
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 759..780
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 243
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 797
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 802
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 806
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:21406692"
FT CROSSLNK 911
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:18655026"
FT VAR_SEQ 1..24
FT /note="MSRRKQRKPQQLISDCEGPSASEN -> MAHESERSSRLGVPCGEPAELG
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056251"
FT VAR_SEQ 131..200
FT /note="GTAAGGGGGLILASPKLGATPLPPESTPAPPPPPPPPPPPGVGSGHLNIPLI
FT LEELRVLQQRQIHQMQMT -> EPVCGIPVKWPAHEALEFQLHLHYHSKPGPTSAVWPR
FT NCGWEGASNNGIQGSQGEDSPPPISASCTQGSA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056252"
FT VAR_SEQ 201..1007
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056253"
FT VARIANT 75
FT /note="S -> C (in dbSNP:rs2242527)"
FT /id="VAR_014129"
FT VARIANT 122
FT /note="P -> S (in dbSNP:rs1263811)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:8975705, ECO:0000269|PubMed:9205841"
FT /id="VAR_014130"
FT VARIANT 746
FT /note="G -> R (in dbSNP:rs1263810)"
FT /evidence="ECO:0000269|PubMed:8975705,
FT ECO:0000269|PubMed:9205841, ECO:0000269|Ref.6"
FT /id="VAR_014131"
FT CONFLICT 547
FT /note="R -> L (in Ref. 1; X98834 and 5; AAI36529/AAI36530)"
FT /evidence="ECO:0000305"
FT CONFLICT 554
FT /note="V -> M (in Ref. 1; X98834)"
FT /evidence="ECO:0000305"
FT CONFLICT 575..581
FT /note="FPYVLEP -> LPLCARA (in Ref. 1; X98834)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1007 AA; 105309 MW; 9F9335CE7939EFA7 CRC64;
MSRRKQRKPQ QLISDCEGPS ASENGDASEE DHPQVCAKCC AQFTDPTEFL AHQNACSTDP
PVMVIIGGQE NPNNSSASSE PRPEGHNNPQ VMDTEHSNPP DSGSSVPTDP TWGPERRGEE
SPGHFLVAAT GTAAGGGGGL ILASPKLGAT PLPPESTPAP PPPPPPPPPP GVGSGHLNIP
LILEELRVLQ QRQIHQMQMT EQICRQVLLL GSLGQTVGAP ASPSELPGTG TASSTKPLLP
LFSPIKPVQT SKTLASSSSS SSSSSGAETP KQAFFHLYHP LGSQHPFSAG GVGRSHKPTP
APSPALPGST DQLIASPHLA FPSTTGLLAA QCLGAARGLE ATASPGLLKP KNGSGELSYG
EVMGPLEKPG GRHKCRFCAK VFGSDSALQI HLRSHTGERP YKCNVCGNRF TTRGNLKVHF
HRHREKYPHV QMNPHPVPEH LDYVITSSGL PYGMSVPPEK AEEEAATPGG GVERKPLVAS
TTALSATESL TLLSTSAGTA TAPGLPAFNK FVLMKAVEPK NKADENTPPG SEGSAISGVA
ESSTATRMQL SKLVTSLPSW ALLTNHFKST GSFPFPYVLE PLGASPSETS KLQQLVEKID
RQGAVAVTSA ASGAPTTSAP APSSSASSGP NQCVICLRVL SCPRALRLHY GQHGGERPFK
CKVCGRAFST RGNLRAHFVG HKASPAARAQ NSCPICQKKF TNAVTLQQHV RMHLGGQIPN
GGTALPEGGG AAQENGSEQS TVSGAGSFPQ QQSQQPSPEE ELSEEEEEED EEEEEDVTDE
DSLAGRGSES GGEKAISVRG DSEEASGAEE EVGTVAAAAT AGKEMDSNEK TTQQSSLPPP
PPPDSLDQPQ PMEQGSSGVL GGKEEGGKPE RSSSPASALT PEGEATSVTL VEELSLQEAM
RKEPGESSSR KACEVCGQAF PSQAALEEHQ KTHPKEGPLF TCVFCRQGFL ERATLKKHML
LAHHQVQPFA PHGPQNIAAL SLVPGCSPSI TSTGLSPFPR KDDPTIP
