CT2NL_HUMAN
ID CT2NL_HUMAN Reviewed; 639 AA.
AC Q9P2B4; B3KMS5; Q96B40;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=CTTNBP2 N-terminal-like protein;
GN Name=CTTNBP2NL; Synonyms=KIAA1433;
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 [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVI. The
RT complete sequences of 150 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:65-73(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-560, 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 SER-488 AND SER-523, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-481; SER-488; SER-523;
RP SER-527 AND THR-590, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [8]
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 [9]
RP INTERACTION WITH MOB4; PPP2R1A; PPP2CB; STK24; STK25; STK26; STRN4; STRIP1
RP AND STRIP2, AND HOMOMERIZATION.
RX PubMed=18782753; DOI=10.1074/mcp.m800266-mcp200;
RA Goudreault M., D'Ambrosio L.M., Kean M.J., Mullin M.J., Larsen B.G.,
RA Sanchez A., Chaudhry S., Chen G.I., Sicheri F., Nesvizhskii A.I.,
RA Aebersold R., Raught B., Gingras A.C.;
RT "A PP2A phosphatase high density interaction network identifies a novel
RT striatin-interacting phosphatase and kinase complex linked to the cerebral
RT cavernous malformation 3 (CCM3) protein.";
RL Mol. Cell. Proteomics 8:157-171(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-488; SER-523; SER-560;
RP SER-563; THR-590 AND SER-592, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-488; SER-560; SER-563 AND
RP THR-570, AND 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284; SER-285; SER-481;
RP SER-488; SER-523; SER-560; SER-563 AND SER-568, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE 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).
CC -!- FUNCTION: Regulates lamellipodial actin dynamics in a CTTN-dependent
CC manner. {ECO:0000250|UniProtKB:Q8SX68}.
CC -!- SUBUNIT: Interacts with CTTN/cortactin; this interaction may
CC redistribute CTTN to stress fibers (By similarity). May form homomers.
CC May interact with MOB4, PPP2R1A, PPP2CB, STK24, STK25, STK26, STRN4,
CC STRIP1 and STRIP2. {ECO:0000250, ECO:0000269|PubMed:18782753}.
CC -!- INTERACTION:
CC Q9P2B4; O14964: HGS; NbExp=3; IntAct=EBI-1774273, EBI-740220;
CC Q9P2B4; O75031: HSF2BP; NbExp=3; IntAct=EBI-1774273, EBI-7116203;
CC Q9P2B4; Q9Y3A3: MOB4; NbExp=6; IntAct=EBI-1774273, EBI-713935;
CC Q9P2B4; Q96KN3: PKNOX2; NbExp=3; IntAct=EBI-1774273, EBI-2692890;
CC Q9P2B4; Q9Y6E0: STK24; NbExp=5; IntAct=EBI-1774273, EBI-740175;
CC Q9P2B4; Q9P289: STK26; NbExp=5; IntAct=EBI-1774273, EBI-618239;
CC Q9P2B4; Q5VSL9: STRIP1; NbExp=4; IntAct=EBI-1774273, EBI-1773588;
CC Q9P2B4; O43815: STRN; NbExp=6; IntAct=EBI-1774273, EBI-1046642;
CC Q9P2B4; Q13033: STRN3; NbExp=8; IntAct=EBI-1774273, EBI-1053857;
CC Q9P2B4; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-1774273, EBI-739895;
CC -!- SUBCELLULAR LOCATION: Cell projection, lamellipodium
CC {ECO:0000250|UniProtKB:Q8SX68}. Cytoplasm, cytoskeleton, stress fiber
CC {ECO:0000250|UniProtKB:Q99LJ0}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA92671.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB037854; BAA92671.1; ALT_INIT; mRNA.
DR EMBL; AK022544; BAG51087.1; -; mRNA.
DR EMBL; AL354760; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC016029; AAH16029.1; -; mRNA.
DR CCDS; CCDS845.1; -.
DR RefSeq; NP_061174.1; NM_018704.2.
DR RefSeq; XP_011540083.1; XM_011541781.2.
DR RefSeq; XP_016857295.1; XM_017001806.1.
DR AlphaFoldDB; Q9P2B4; -.
DR SMR; Q9P2B4; -.
DR BioGRID; 121000; 68.
DR IntAct; Q9P2B4; 46.
DR MINT; Q9P2B4; -.
DR STRING; 9606.ENSP00000271277; -.
DR GlyGen; Q9P2B4; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9P2B4; -.
DR PhosphoSitePlus; Q9P2B4; -.
DR BioMuta; CTTNBP2NL; -.
DR DMDM; 92087169; -.
DR EPD; Q9P2B4; -.
DR jPOST; Q9P2B4; -.
DR MassIVE; Q9P2B4; -.
DR MaxQB; Q9P2B4; -.
DR PaxDb; Q9P2B4; -.
DR PeptideAtlas; Q9P2B4; -.
DR PRIDE; Q9P2B4; -.
DR ProteomicsDB; 83766; -.
DR Antibodypedia; 2021; 109 antibodies from 23 providers.
DR DNASU; 55917; -.
DR Ensembl; ENST00000271277.11; ENSP00000271277.6; ENSG00000143079.15.
DR GeneID; 55917; -.
DR KEGG; hsa:55917; -.
DR MANE-Select; ENST00000271277.11; ENSP00000271277.6; NM_018704.3; NP_061174.1.
DR UCSC; uc001ebx.4; human.
DR CTD; 55917; -.
DR DisGeNET; 55917; -.
DR GeneCards; CTTNBP2NL; -.
DR HGNC; HGNC:25330; CTTNBP2NL.
DR HPA; ENSG00000143079; Low tissue specificity.
DR MIM; 615100; gene.
DR neXtProt; NX_Q9P2B4; -.
DR OpenTargets; ENSG00000143079; -.
DR PharmGKB; PA142672062; -.
DR VEuPathDB; HostDB:ENSG00000143079; -.
DR eggNOG; KOG1103; Eukaryota.
DR GeneTree; ENSGT00950000182852; -.
DR HOGENOM; CLU_028813_1_0_1; -.
DR InParanoid; Q9P2B4; -.
DR OMA; MLVMECK; -.
DR OrthoDB; 660559at2759; -.
DR PhylomeDB; Q9P2B4; -.
DR TreeFam; TF325130; -.
DR PathwayCommons; Q9P2B4; -.
DR SignaLink; Q9P2B4; -.
DR SIGNOR; Q9P2B4; -.
DR BioGRID-ORCS; 55917; 10 hits in 1072 CRISPR screens.
DR ChiTaRS; CTTNBP2NL; human.
DR GeneWiki; CTTNBP2NL; -.
DR GenomeRNAi; 55917; -.
DR Pharos; Q9P2B4; Tbio.
DR PRO; PR:Q9P2B4; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9P2B4; protein.
DR Bgee; ENSG00000143079; Expressed in secondary oocyte and 188 other tissues.
DR ExpressionAtlas; Q9P2B4; baseline and differential.
DR Genevisible; Q9P2B4; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:LIFEdb.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0051721; F:protein phosphatase 2A binding; IDA:MGI.
DR GO; GO:0034763; P:negative regulation of transmembrane transport; IMP:MGI.
DR GO; GO:0032410; P:negative regulation of transporter activity; IMP:MGI.
DR GO; GO:0006470; P:protein dephosphorylation; IMP:MGI.
DR InterPro; IPR019131; Cortactin-binding_p2_N.
DR Pfam; PF09727; CortBP2; 1.
PE 1: Evidence at protein level;
KW Cell projection; Coiled coil; Cytoplasm; Cytoskeleton; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..639
FT /note="CTTNBP2 N-terminal-like protein"
FT /id="PRO_0000226997"
FT REGION 387..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 463..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 511..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 87..285
FT /evidence="ECO:0000255"
FT COMPBIAS 402..430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..564
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..591
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..609
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 284
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 285
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 481
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 488
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 523
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 527
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 560
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 563
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 568
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 570
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 590
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 592
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT VARIANT 296
FT /note="V -> M (in dbSNP:rs1175640)"
FT /id="VAR_050925"
FT VARIANT 409
FT /note="S -> G (in dbSNP:rs12137578)"
FT /id="VAR_050926"
FT CONFLICT 38
FT /note="D -> V (in Ref. 2; BAG51087)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 639 AA; 70158 MW; 63F1D27C50623564 CRC64;
MNLEKLSKPE LLTLFSILEG ELEARDLVIE ALKAQHRDTF IEERYGKYNI SDPLMALQRD
FETLKEKNDG EKQPVCTNPL SILKVVMKQC KNMQERMLSQ LAAAESRHRK VILDLEEERQ
RHAQDTAEGD DVTYMLEKER ERLTQQLEFE KSQVKKFEKE QKKLSSQLEE ERSRHKQLSS
MLVLECKKAT NKAAEEGQKA GELSLKLEKE KSRVSKLEEE LAAERKRGLQ TEAQVEKQLS
EFDIEREQLR AKLNREENRT KTLKEEMESL KKIVKDLEAS HQHSSPNEQL KKPVTVSKGT
ATEPLMLMSV FCQTESFPAE RTHGSNIAKM TNTGLPGPAT PAYSYAKTNG HCDPEIQTTR
ELTAGNNVEN QVPPREKSVA LAQEKPVENG GCPVGIETPV PMPSPLSSSG SSLSPSSTAS
SSLTSSPCSS PVLTKRLLGS SASSPGYQSS YQVGINQRFH AARHKFQSQA DQDQQASGLQ
SPPSRDLSPT LIDNSAAKQL ARNTVTQVLS RFTSQQGPIK PVSPNSSPFG TDYRNLANTA
NPRGDTSHSP TPGKVSSPLS PLSPGIKSPT IPRAERGNPP PIPPKKPGLT PSPSATTPLT
KTHSQAASLT TAEDLASSCS SNTVVANGKD VELLLPTSS
