SUGP2_HUMAN
ID SUGP2_HUMAN Reviewed; 1082 AA.
AC Q8IX01; C9JI71; O15071; O60369; Q5JPH7; Q8WUF7;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=SURP and G-patch domain-containing protein 2;
DE AltName: Full=Arginine/serine-rich-splicing factor 14;
DE AltName: Full=Splicing factor, arginine/serine-rich 14;
GN Name=SUGP2; Synonyms=KIAA0365, SFRS14;
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), ALTERNATIVE SPLICING, TISSUE
RP SPECIFICITY, AND VARIANT SER-206.
RX PubMed=12594045; DOI=10.1016/s0378-1119(02)01230-1;
RA Sampson N.D., Hewitt J.E.;
RT "SF4 and SFRS14, two related putative splicing factors on human chromosome
RT 19p13.11.";
RL Gene 305:91-100(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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.
RA Ohara O., Nagase T., Kikuno R., Nomura N.;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4), AND VARIANT
RP SER-206.
RC TISSUE=Endometrial tumor, and Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT SER-206.
RC TISSUE=Duodenum;
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-7, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-275 AND SER-277, 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 [9]
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 [10]
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 [11]
RP 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 [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96; SER-224; SER-315; SER-573
RP AND SER-603, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-573 AND SER-754, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [15]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-228; LYS-305 AND LYS-650, 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 [16]
RP STRUCTURE BY NMR OF 587-639.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of SURP domain in SFRS14 protein.";
RL Submitted (NOV-2005) to the PDB data bank.
CC -!- FUNCTION: May play a role in mRNA splicing. {ECO:0000305}.
CC -!- INTERACTION:
CC Q8IX01-3; Q08379: GOLGA2; NbExp=3; IntAct=EBI-12317645, EBI-618309;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8IX01-1; Sequence=Displayed;
CC Name=3;
CC IsoId=Q8IX01-3; Sequence=VSP_013112, VSP_013113;
CC Name=4;
CC IsoId=Q8IX01-4; Sequence=VSP_013112;
CC -!- TISSUE SPECIFICITY: Detected in adult testis, and in fetal brain and
CC kidney. {ECO:0000269|PubMed:12594045}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC06129.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAH20586.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA20820.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF518874; AAN77117.1; -; mRNA.
DR EMBL; AB002363; BAA20820.2; ALT_INIT; mRNA.
DR EMBL; BX647813; CAI46012.1; -; mRNA.
DR EMBL; AL832488; CAI46117.1; -; mRNA.
DR EMBL; AC004447; AAC06129.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC020586; AAH20586.1; ALT_INIT; mRNA.
DR CCDS; CCDS12392.1; -. [Q8IX01-1]
DR PIR; T03030; T03030.
DR RefSeq; NP_001017392.2; NM_001017392.4. [Q8IX01-1]
DR RefSeq; NP_001308626.1; NM_001321697.1. [Q8IX01-1]
DR RefSeq; NP_055699.2; NM_014884.4. [Q8IX01-1]
DR RefSeq; XP_016881626.1; XM_017026137.1.
DR PDB; 1X4P; NMR; -; A=587-639.
DR PDBsum; 1X4P; -.
DR AlphaFoldDB; Q8IX01; -.
DR SMR; Q8IX01; -.
DR BioGRID; 115449; 186.
DR IntAct; Q8IX01; 46.
DR MINT; Q8IX01; -.
DR STRING; 9606.ENSP00000472286; -.
DR GlyGen; Q8IX01; 3 sites, 1 O-linked glycan (3 sites).
DR iPTMnet; Q8IX01; -.
DR PhosphoSitePlus; Q8IX01; -.
DR BioMuta; SUGP2; -.
DR DMDM; 308153496; -.
DR EPD; Q8IX01; -.
DR jPOST; Q8IX01; -.
DR MassIVE; Q8IX01; -.
DR MaxQB; Q8IX01; -.
DR PaxDb; Q8IX01; -.
DR PeptideAtlas; Q8IX01; -.
DR PRIDE; Q8IX01; -.
DR ProteomicsDB; 70947; -. [Q8IX01-1]
DR ProteomicsDB; 70948; -. [Q8IX01-3]
DR ProteomicsDB; 70949; -. [Q8IX01-4]
DR Antibodypedia; 28312; 159 antibodies from 26 providers.
DR DNASU; 10147; -.
DR Ensembl; ENST00000330854.15; ENSP00000332373.10; ENSG00000064607.17. [Q8IX01-4]
DR Ensembl; ENST00000337018.10; ENSP00000337926.5; ENSG00000064607.17. [Q8IX01-1]
DR Ensembl; ENST00000452918.7; ENSP00000389380.1; ENSG00000064607.17. [Q8IX01-1]
DR Ensembl; ENST00000594773.5; ENSP00000470915.1; ENSG00000064607.17. [Q8IX01-3]
DR Ensembl; ENST00000601879.5; ENSP00000472286.1; ENSG00000064607.17. [Q8IX01-1]
DR GeneID; 10147; -.
DR KEGG; hsa:10147; -.
DR MANE-Select; ENST00000452918.7; ENSP00000389380.1; NM_001017392.5; NP_001017392.2.
DR UCSC; uc002nkx.3; human. [Q8IX01-1]
DR CTD; 10147; -.
DR DisGeNET; 10147; -.
DR GeneCards; SUGP2; -.
DR HGNC; HGNC:18641; SUGP2.
DR HPA; ENSG00000064607; Low tissue specificity.
DR MIM; 607993; gene.
DR neXtProt; NX_Q8IX01; -.
DR OpenTargets; ENSG00000064607; -.
DR PharmGKB; PA165394371; -.
DR VEuPathDB; HostDB:ENSG00000064607; -.
DR eggNOG; KOG0965; Eukaryota.
DR GeneTree; ENSGT00410000025695; -.
DR HOGENOM; CLU_010012_0_0_1; -.
DR InParanoid; Q8IX01; -.
DR OMA; CPSIRFT; -.
DR OrthoDB; 1232201at2759; -.
DR PhylomeDB; Q8IX01; -.
DR TreeFam; TF326321; -.
DR PathwayCommons; Q8IX01; -.
DR SignaLink; Q8IX01; -.
DR BioGRID-ORCS; 10147; 25 hits in 1082 CRISPR screens.
DR ChiTaRS; SUGP2; human.
DR EvolutionaryTrace; Q8IX01; -.
DR GeneWiki; SFRS14; -.
DR GenomeRNAi; 10147; -.
DR Pharos; Q8IX01; Tdark.
DR PRO; PR:Q8IX01; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q8IX01; protein.
DR Bgee; ENSG00000064607; Expressed in left testis and 202 other tissues.
DR ExpressionAtlas; Q8IX01; baseline and differential.
DR Genevisible; Q8IX01; HS.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.790; -; 2.
DR InterPro; IPR000467; G_patch_dom.
DR InterPro; IPR040169; SUGP1/2.
DR InterPro; IPR000061; Surp.
DR InterPro; IPR035967; SWAP/Surp_sf.
DR PANTHER; PTHR23340; PTHR23340; 1.
DR Pfam; PF01585; G-patch; 1.
DR Pfam; PF01805; Surp; 1.
DR SMART; SM00443; G_patch; 1.
DR SMART; SM00648; SWAP; 2.
DR SUPFAM; SSF109905; SSF109905; 2.
DR PROSITE; PS50174; G_PATCH; 1.
DR PROSITE; PS50128; SURP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Isopeptide bond; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Ubl conjugation.
FT CHAIN 1..1082
FT /note="SURP and G-patch domain-containing protein 2"
FT /id="PRO_0000097708"
FT REPEAT 590..633
FT /note="SURP motif 1"
FT REPEAT 787..830
FT /note="SURP motif 2"
FT DOMAIN 1011..1057
FT /note="G-patch"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00092"
FT REGION 65..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 694..779
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 849..930
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 982..1002
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1030..1061
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 995..1000
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 695..709
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 849..864
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 888..905
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 7
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 224
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 275
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 277
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 573
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 603
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 754
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 757
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CH09"
FT MOD_RES 863
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CH09"
FT CROSSLNK 228
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 650
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 890..941
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_013112"
FT VAR_SEQ 1044..1082
FT /note="GTPSEGEGLGADGQEHKEDTFDVFRQRMMQMYRHKRANK -> YAAGSLGWE
FT WVGPQSFHLQPAAWLLHSQDGLQLAVDFCFLNRRHLQMRS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013113"
FT VARIANT 206
FT /note="G -> S (in dbSNP:rs4808907)"
FT /evidence="ECO:0000269|PubMed:12594045,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17974005"
FT /id="VAR_023711"
FT VARIANT 552
FT /note="M -> T (in dbSNP:rs10404860)"
FT /id="VAR_051341"
FT VARIANT 649
FT /note="Q -> R (in dbSNP:rs10414535)"
FT /id="VAR_051342"
FT VARIANT 722
FT /note="Q -> R (in dbSNP:rs34540303)"
FT /id="VAR_051343"
FT VARIANT 881
FT /note="R -> Q (in dbSNP:rs35646935)"
FT /id="VAR_051344"
FT HELIX 588..599
FT /evidence="ECO:0007829|PDB:1X4P"
FT HELIX 604..612
FT /evidence="ECO:0007829|PDB:1X4P"
FT HELIX 614..616
FT /evidence="ECO:0007829|PDB:1X4P"
FT TURN 618..620
FT /evidence="ECO:0007829|PDB:1X4P"
FT STRAND 623..625
FT /evidence="ECO:0007829|PDB:1X4P"
FT HELIX 626..639
FT /evidence="ECO:0007829|PDB:1X4P"
SQ SEQUENCE 1082 AA; 120207 MW; 619AE0AC087761BD CRC64;
MAARRITQET FDAVLQEKAK RYHMDASGEA VSETLQFKAQ DLLRAVPRSR AEMYDDVHSD
GRYSLSGSVA HSRDAGREGL RSDVFPGPSF RSSNPSISDD SYFRKECGRD LEFSHSDSRD
QVIGHRKLGH FRSQDWKFAL RGSWEQDFGH PVSQESSWSQ EYSFGPSAVL GDFGSSRLIE
KECLEKESRD YDVDHPGEAD SVLRGGSQVQ ARGRALNIVD QEGSLLGKGE TQGLLTAKGG
VGKLVTLRNV STKKIPTVNR ITPKTQGTNQ IQKNTPSPDV TLGTNPGTED IQFPIQKIPL
GLDLKNLRLP RRKMSFDIID KSDVFSRFGI EIIKWAGFHT IKDDIKFSQL FQTLFELETE
TCAKMLASFK CSLKPEHRDF CFFTIKFLKH SALKTPRVDN EFLNMLLDKG AVKTKNCFFE
IIKPFDKYIM RLQDRLLKSV TPLLMACNAY ELSVKMKTLS NPLDLALALE TTNSLCRKSL
ALLGQTFSLA SSFRQEKILE AVGLQDIAPS PAAFPNFEDS TLFGREYIDH LKAWLVSSGC
PLQVKKAEPE PMREEEKMIP PTKPEIQAKA PSSLSDAVPQ RADHRVVGTI DQLVKRVIEG
SLSPKERTLL KEDPAYWFLS DENSLEYKYY KLKLAEMQRM SENLRGADQK PTSADCAVRA
MLYSRAVRNL KKKLLPWQRR GLLRAQGLRG WKARRATTGT QTLLSSGTRL KHHGRQAPGL
SQAKPSLPDR NDAAKDCPPD PVGPSPQDPS LEASGPSPKP AGVDISEAPQ TSSPCPSADI
DMKTMETAEK LARFVAQVGP EIEQFSIENS TDNPDLWFLH DQNSSAFKFY RKKVFELCPS
ICFTSSPHNL HTGGGDTTGS QESPVDLMEG EAEFEDEPPP REAELESPEV MPEEEDEDDE
DGGEEAPAPG GAGKSEGSTP ADGLPGEAAE DDLAGAPALS QASSGTCFPR KRISSKSLKV
GMIPAPKRVC LIQEPKVHEP VRIAYDRPRG RPMSKKKKPK DLDFAQQKLT DKNLGFQMLQ
KMGWKEGHGL GSLGKGIREP VSVGTPSEGE GLGADGQEHK EDTFDVFRQR MMQMYRHKRA
NK
