CTSL2_HUMAN
ID CTSL2_HUMAN Reviewed; 466 AA.
AC Q05D32; Q3ZTU1; Q6AI06; Q8IYI9; Q9NVT2; Q9NZX8; Q9P030;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=CTD small phosphatase-like protein 2;
DE Short=CTDSP-like 2;
DE EC=3.1.3.-;
GN Name=CTDSPL2; ORFNames=HSPC058, HSPC129;
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).
RX PubMed=16533400; DOI=10.1186/1471-2164-7-48;
RA Kemmer D., Podowski R.M., Arenillas D., Lim J., Hodges E., Roth P.,
RA Sonnhammer E.L.L., Hoeoeg C., Wasserman W.W.;
RT "NovelFam3000 -- uncharacterized human protein domains conserved across
RT model organisms.";
RL BMC Genomics 7:48-48(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Zhang J.W., Zhang X., Ma Y.N.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Teratocarcinoma;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Bone marrow;
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, 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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85; THR-86; SER-104 AND
RP SER-165, AND 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 [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-86; SER-134 AND SER-165, 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 [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-26 AND LYS-57, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-86; SER-104; SER-134 AND
RP SER-165, AND 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104 AND SER-165, 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28; SER-51; THR-86; SER-104;
RP SER-134 AND SER-165, 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 [17]
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).
CC -!- FUNCTION: Probable phosphatase. {ECO:0000250}.
CC -!- INTERACTION:
CC Q05D32; O00629: KPNA4; NbExp=3; IntAct=EBI-10039222, EBI-396343;
CC Q05D32; Q8N165: PDIK1L; NbExp=10; IntAct=EBI-10039222, EBI-6423298;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q05D32-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q05D32-2; Sequence=VSP_033218;
CC -!- SIMILARITY: Belongs to the CTDSPL2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF29030.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAH18623.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=BAA91664.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY364237; AAQ76796.1; -; mRNA.
DR EMBL; DQ128104; AAZ42188.1; -; mRNA.
DR EMBL; AF161543; AAF29030.1; ALT_FRAME; mRNA.
DR EMBL; AF161478; AAF29093.1; -; mRNA.
DR EMBL; AK001385; BAA91664.1; ALT_INIT; mRNA.
DR EMBL; AK291230; BAF83919.1; -; mRNA.
DR EMBL; CR627421; CAH10508.1; -; mRNA.
DR EMBL; CH471082; EAW77265.1; -; Genomic_DNA.
DR EMBL; BC018623; AAH18623.1; ALT_SEQ; mRNA.
DR EMBL; BC035744; AAH35744.1; -; mRNA.
DR CCDS; CCDS10110.1; -. [Q05D32-1]
DR RefSeq; NP_057480.2; NM_016396.2. [Q05D32-1]
DR RefSeq; XP_005254498.1; XM_005254441.2. [Q05D32-1]
DR RefSeq; XP_006720628.1; XM_006720565.2. [Q05D32-1]
DR AlphaFoldDB; Q05D32; -.
DR SMR; Q05D32; -.
DR BioGRID; 119571; 58.
DR IntAct; Q05D32; 25.
DR MINT; Q05D32; -.
DR STRING; 9606.ENSP00000260327; -.
DR DEPOD; CTDSPL2; -.
DR iPTMnet; Q05D32; -.
DR PhosphoSitePlus; Q05D32; -.
DR BioMuta; CTDSPL2; -.
DR DMDM; 187471086; -.
DR EPD; Q05D32; -.
DR jPOST; Q05D32; -.
DR MassIVE; Q05D32; -.
DR MaxQB; Q05D32; -.
DR PaxDb; Q05D32; -.
DR PeptideAtlas; Q05D32; -.
DR PRIDE; Q05D32; -.
DR ProteomicsDB; 58398; -. [Q05D32-1]
DR ProteomicsDB; 58399; -. [Q05D32-2]
DR Antibodypedia; 42444; 147 antibodies from 27 providers.
DR DNASU; 51496; -.
DR Ensembl; ENST00000260327.9; ENSP00000260327.4; ENSG00000137770.14. [Q05D32-1]
DR Ensembl; ENST00000558373.5; ENSP00000453051.1; ENSG00000137770.14. [Q05D32-2]
DR Ensembl; ENST00000558966.5; ENSP00000452837.1; ENSG00000137770.14. [Q05D32-1]
DR GeneID; 51496; -.
DR KEGG; hsa:51496; -.
DR MANE-Select; ENST00000260327.9; ENSP00000260327.4; NM_016396.3; NP_057480.2.
DR UCSC; uc001ztr.4; human. [Q05D32-1]
DR CTD; 51496; -.
DR DisGeNET; 51496; -.
DR GeneCards; CTDSPL2; -.
DR HGNC; HGNC:26936; CTDSPL2.
DR HPA; ENSG00000137770; Low tissue specificity.
DR MIM; 618739; gene.
DR neXtProt; NX_Q05D32; -.
DR OpenTargets; ENSG00000137770; -.
DR PharmGKB; PA142672063; -.
DR VEuPathDB; HostDB:ENSG00000137770; -.
DR eggNOG; KOG1605; Eukaryota.
DR GeneTree; ENSGT01040000240503; -.
DR HOGENOM; CLU_034042_4_0_1; -.
DR InParanoid; Q05D32; -.
DR OMA; PKKQLVX; -.
DR PhylomeDB; Q05D32; -.
DR TreeFam; TF354278; -.
DR PathwayCommons; Q05D32; -.
DR SignaLink; Q05D32; -.
DR SIGNOR; Q05D32; -.
DR BioGRID-ORCS; 51496; 84 hits in 1054 CRISPR screens.
DR ChiTaRS; CTDSPL2; human.
DR GenomeRNAi; 51496; -.
DR Pharos; Q05D32; Tbio.
DR PRO; PR:Q05D32; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q05D32; protein.
DR Bgee; ENSG00000137770; Expressed in calcaneal tendon and 178 other tissues.
DR ExpressionAtlas; Q05D32; baseline and differential.
DR Genevisible; Q05D32; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IBA:GO_Central.
DR GO; GO:0008420; F:RNA polymerase II CTD heptapeptide repeat phosphatase activity; IDA:CACAO.
DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; IEA:Ensembl.
DR GO; GO:0046827; P:positive regulation of protein export from nucleus; IEA:Ensembl.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:Ensembl.
DR GO; GO:0006611; P:protein export from nucleus; IEA:Ensembl.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR011948; Dullard_phosphatase.
DR InterPro; IPR004274; FCP1_dom.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR Pfam; PF03031; NIF; 1.
DR SMART; SM00577; CPDc; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR02251; HIF-SF_euk; 1.
DR PROSITE; PS50969; FCP1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Hydrolase; Phosphoprotein;
KW Protein phosphatase; Reference proteome.
FT CHAIN 1..466
FT /note="CTD small phosphatase-like protein 2"
FT /id="PRO_0000331464"
FT DOMAIN 283..442
FT /note="FCP1 homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00336"
FT REGION 1..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 220..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..140
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 26
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 57
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 86
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 134
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT VAR_SEQ 159..230
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_033218"
FT VARIANT 244
FT /note="A -> V (in dbSNP:rs871923)"
FT /id="VAR_042886"
FT CONFLICT 107..110
FT /note="NGEA -> MEKL (in Ref. 3; AAF29093)"
FT /evidence="ECO:0000305"
FT CONFLICT 228
FT /note="P -> T (in Ref. 3; AAF29030)"
FT /evidence="ECO:0000305"
FT CONFLICT 321
FT /note="I -> V (in Ref. 1; AAQ76796 and 4; BAA91664)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 466 AA; 52999 MW; E8BA6911EBD4B332 CRC64;
MRLRTRKASQ QSNQIQTQRT ARAKRKYSEV DDSLPSGGEK PSKNETGLLS SIKKFIKGST
PKEERENPSK RSRIERDIDN NLITSTPRAG EKPNKQISRV RRKSQVNGEA GSYEMTNQHV
KQNGKLEDNP SSGSPPRTTL LGTIFSPVFN FFSPANKNGT SGSDSPGQAV EAEEIVKQLD
MEQVDEITTS TTTSTNGAAY SNQAVQVRPS LNNGLEEAEE TVNRDIPPLT APVTPDSGYS
SAHAEATYEE DWEVFDPYYF IKHVPPLTEE QLNRKPALPL KTRSTPEFSL VLDLDETLVH
CSLNELEDAA LTFPVLFQDV IYQVYVRLRP FFREFLERMS QMYEIILFTA SKKVYADKLL
NILDPKKQLV RHRLFREHCV CVQGNYIKDL NILGRDLSKT IIIDNSPQAF AYQLSNGIPI
ESWFMDKNDN ELLKLIPFLE KLVELNEDVR PHIRDRFRLH DLLPPD
