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 24-JAN-2024, entry version 159. 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}; 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; 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; 74. 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; 9606-ENSP00000271277; -. DR PeptideAtlas; Q9P2B4; -. DR ProteomicsDB; 83766; -. DR Pumba; Q9P2B4; -. DR Antibodypedia; 2021; 115 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 AGR; HGNC:25330; -. 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; ANGHFEP; -. DR OrthoDB; 5395797at2759; -. DR PhylomeDB; Q9P2B4; -. DR TreeFam; TF325130; -. DR PathwayCommons; Q9P2B4; -. DR SignaLink; Q9P2B4; -. DR SIGNOR; Q9P2B4; -. DR BioGRID-ORCS; 55917; 11 hits in 1150 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 190 other cell types or tissues. DR ExpressionAtlas; Q9P2B4; baseline and differential. 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:0001725; C:stress fiber; 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 PANTHER; PTHR23166:SF9; CTTNBP2 N-TERMINAL-LIKE PROTEIN; 1. DR PANTHER; PTHR23166; FILAMIN/GPBP-INTERACTING PROTEIN; 1. DR Pfam; PF09727; CortBP2; 1. DR Genevisible; Q9P2B4; HS. 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 //