AF1L2_HUMAN
ID AF1L2_HUMAN Reviewed; 818 AA.
AC Q8N4X5; A8K6P7; B3KVQ8; Q2UZW3; Q8TB54; Q96PX4; Q96SY5;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Actin filament-associated protein 1-like 2;
DE Short=AFAP1-like protein 2;
GN Name=AFAP1L2; Synonyms=KIAA1914, XB130;
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).
RA Bai X.-H., Keshavjee S., Liu M.;
RT "XB130, a novel adaptor protein for Src binding and activation.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain;
RX PubMed=11572484; DOI=10.1093/dnares/8.4.179;
RA Nagase T., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XXI. The
RT complete sequences of 60 new cDNA clones from brain which code for large
RT proteins.";
RL DNA Res. 8:179-187(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC TISSUE=Cerebellum, and Placenta;
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] (ISOFORMS 1 AND 2).
RC TISSUE=Pancreas;
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 FUNCTION, INTERACTION WITH SRC, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP MUTAGENESIS OF TYR-4, AND PHOSPHORYLATION.
RX PubMed=17412687; DOI=10.1074/jbc.m701684200;
RA Xu J., Bai X.-H., Lodyga M., Han B., Xiao H., Keshavjee S., Hu J.,
RA Zhang H., Yang B.B., Liu M.;
RT "XB130, a novel adaptor protein for signal transduction.";
RL J. Biol. Chem. 282:16401-16412(2007).
RN [7]
RP PHOSPHORYLATION, INTERACTION WITH LCK, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=18844995; DOI=10.1186/1478-811x-6-7;
RA Emaduddin M., Edelmann M.J., Kessler B.M., Feller S.M.;
RT "Odin (ANKS1A) is a Src family kinase target in colorectal cancer cells.";
RL Cell Commun. Signal. 6:7-7(2008).
RN [8]
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 [9]
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 [10]
RP STRUCTURE BY NMR OF 354-448.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the C-terminal PH domain of hypothetical protein
RT KIAA1914 from human.";
RL Submitted (NOV-2005) to the PDB data bank.
CC -!- FUNCTION: May play a role in a signaling cascade by enhancing the
CC kinase activity of SRC. Contributes to SRC-regulated transcription
CC activation. {ECO:0000269|PubMed:17412687}.
CC -!- SUBUNIT: Interacts with SRC. Interacts with LCK when tyrosine
CC phosphorylated. {ECO:0000269|PubMed:17412687,
CC ECO:0000269|PubMed:18844995}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17412687}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q8N4X5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8N4X5-2; Sequence=VSP_014255;
CC Name=3;
CC IsoId=Q8N4X5-3; Sequence=VSP_014254, VSP_014256;
CC Name=4;
CC IsoId=Q8N4X5-4; Sequence=VSP_036211, VSP_014255;
CC -!- TISSUE SPECIFICITY: Detected in spleen and thyroid, and at lower levels
CC in kidney, brain, lung and pancreas. {ECO:0000269|PubMed:17412687}.
CC -!- PTM: Tyrosine phosphorylated (by SRC). {ECO:0000269|PubMed:17412687,
CC ECO:0000269|PubMed:18844995}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB67807.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF474151; AAQ05765.1; -; mRNA.
DR EMBL; AB067501; BAB67807.1; ALT_INIT; mRNA.
DR EMBL; AC005383; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL133384; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL355302; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK027470; BAB55135.1; -; mRNA.
DR EMBL; AK291712; BAF84401.1; -; mRNA.
DR EMBL; AK123108; BAG53870.1; -; mRNA.
DR EMBL; BC024314; AAH24314.1; -; mRNA.
DR EMBL; BC033212; AAH33212.1; -; mRNA.
DR CCDS; CCDS31286.1; -. [Q8N4X5-1]
DR CCDS; CCDS31287.1; -. [Q8N4X5-2]
DR RefSeq; NP_001001936.1; NM_001001936.2. [Q8N4X5-1]
DR RefSeq; NP_001274753.1; NM_001287824.1.
DR RefSeq; NP_115939.1; NM_032550.3. [Q8N4X5-2]
DR PDB; 2COF; NMR; -; A=354-447.
DR PDBsum; 2COF; -.
DR AlphaFoldDB; Q8N4X5; -.
DR BMRB; Q8N4X5; -.
DR SMR; Q8N4X5; -.
DR BioGRID; 124161; 13.
DR IntAct; Q8N4X5; 7.
DR STRING; 9606.ENSP00000303042; -.
DR GlyGen; Q8N4X5; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8N4X5; -.
DR PhosphoSitePlus; Q8N4X5; -.
DR BioMuta; AFAP1L2; -.
DR DMDM; 68052360; -.
DR EPD; Q8N4X5; -.
DR jPOST; Q8N4X5; -.
DR MassIVE; Q8N4X5; -.
DR MaxQB; Q8N4X5; -.
DR PaxDb; Q8N4X5; -.
DR PeptideAtlas; Q8N4X5; -.
DR PRIDE; Q8N4X5; -.
DR ProteomicsDB; 71986; -. [Q8N4X5-1]
DR ProteomicsDB; 71987; -. [Q8N4X5-2]
DR ProteomicsDB; 71988; -. [Q8N4X5-3]
DR ProteomicsDB; 71989; -. [Q8N4X5-4]
DR Antibodypedia; 31934; 135 antibodies from 34 providers.
DR DNASU; 84632; -.
DR Ensembl; ENST00000304129.9; ENSP00000303042.4; ENSG00000169129.15. [Q8N4X5-1]
DR Ensembl; ENST00000369271.7; ENSP00000358276.3; ENSG00000169129.15. [Q8N4X5-2]
DR GeneID; 84632; -.
DR KEGG; hsa:84632; -.
DR MANE-Select; ENST00000304129.9; ENSP00000303042.4; NM_001001936.3; NP_001001936.1.
DR UCSC; uc001lbn.5; human. [Q8N4X5-1]
DR CTD; 84632; -.
DR DisGeNET; 84632; -.
DR GeneCards; AFAP1L2; -.
DR HGNC; HGNC:25901; AFAP1L2.
DR HPA; ENSG00000169129; Tissue enhanced (lymphoid tissue, parathyroid gland, thyroid gland).
DR MIM; 612420; gene.
DR neXtProt; NX_Q8N4X5; -.
DR OpenTargets; ENSG00000169129; -.
DR PharmGKB; PA162375773; -.
DR VEuPathDB; HostDB:ENSG00000169129; -.
DR eggNOG; ENOG502QQA8; Eukaryota.
DR GeneTree; ENSGT00950000183067; -.
DR HOGENOM; CLU_014418_0_0_1; -.
DR InParanoid; Q8N4X5; -.
DR OMA; FLLMQRK; -.
DR OrthoDB; 256810at2759; -.
DR PhylomeDB; Q8N4X5; -.
DR TreeFam; TF332622; -.
DR PathwayCommons; Q8N4X5; -.
DR SignaLink; Q8N4X5; -.
DR SIGNOR; Q8N4X5; -.
DR BioGRID-ORCS; 84632; 9 hits in 1073 CRISPR screens.
DR ChiTaRS; AFAP1L2; human.
DR EvolutionaryTrace; Q8N4X5; -.
DR GenomeRNAi; 84632; -.
DR Pharos; Q8N4X5; Tbio.
DR PRO; PR:Q8N4X5; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q8N4X5; protein.
DR Bgee; ENSG00000169129; Expressed in sural nerve and 143 other tissues.
DR ExpressionAtlas; Q8N4X5; baseline and differential.
DR Genevisible; Q8N4X5; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:HGNC-UCL.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0030296; F:protein tyrosine kinase activator activity; IDA:HGNC-UCL.
DR GO; GO:0042169; F:SH2 domain binding; IPI:HGNC-UCL.
DR GO; GO:0017124; F:SH3 domain binding; IPI:HGNC-UCL.
DR GO; GO:0035591; F:signaling adaptor activity; IEA:InterPro.
DR GO; GO:0006954; P:inflammatory response; IDA:HGNC-UCL.
DR GO; GO:0045742; P:positive regulation of epidermal growth factor receptor signaling pathway; IDA:HGNC-UCL.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; IDA:HGNC-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:HGNC-UCL.
DR GO; GO:0032675; P:regulation of interleukin-6 production; IDA:HGNC-UCL.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; IDA:HGNC-UCL.
DR Gene3D; 2.30.29.30; -; 2.
DR InterPro; IPR030113; AFAP.
DR InterPro; IPR030115; AFAP1L2.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR14338; PTHR14338; 1.
DR PANTHER; PTHR14338:SF4; PTHR14338:SF4; 1.
DR Pfam; PF00169; PH; 2.
DR SMART; SM00233; PH; 2.
DR PROSITE; PS50003; PH_DOMAIN; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Cytoplasm; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..818
FT /note="Actin filament-associated protein 1-like 2"
FT /id="PRO_0000050805"
FT DOMAIN 175..271
FT /note="PH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 353..447
FT /note="PH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 66..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 513..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 765..787
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 652..749
FT /evidence="ECO:0000255"
FT MOD_RES 56
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q5DTU0"
FT MOD_RES 408
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5DTU0"
FT MOD_RES 413
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q5DTU0"
FT MOD_RES 484
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5DTU0"
FT VAR_SEQ 1..478
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11572484"
FT /id="VSP_014254"
FT VAR_SEQ 135
FT /note="N -> NGHSGGFLPTGVPRWVQVPERVIYATITL (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_036211"
FT VAR_SEQ 766..769
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_014255"
FT VAR_SEQ 811..818
FT /note="EWEKKGAS -> VSSHSQPPLGPAEMSLR (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11572484"
FT /id="VSP_014256"
FT VARIANT 138
FT /note="G -> R (in dbSNP:rs11196689)"
FT /id="VAR_050505"
FT VARIANT 366
FT /note="S -> R (in dbSNP:rs7075067)"
FT /id="VAR_050506"
FT VARIANT 522
FT /note="T -> S (in dbSNP:rs2781806)"
FT /id="VAR_050507"
FT VARIANT 726
FT /note="E -> K (in dbSNP:rs11599051)"
FT /id="VAR_054214"
FT MUTAGEN 4
FT /note="Y->F: Reduced interaction with SRC."
FT /evidence="ECO:0000269|PubMed:17412687"
FT CONFLICT 13
FT /note="E -> K (in Ref. 4; BAF84401)"
FT /evidence="ECO:0000305"
FT CONFLICT 224
FT /note="S -> G (in Ref. 4; BAF84401)"
FT /evidence="ECO:0000305"
FT CONFLICT 567
FT /note="N -> D (in Ref. 4; BAB55135)"
FT /evidence="ECO:0000305"
FT CONFLICT 596
FT /note="Missing (in Ref. 4; BAB55135)"
FT /evidence="ECO:0000305"
FT CONFLICT 605
FT /note="D -> Y (in Ref. 4; BAB55135)"
FT /evidence="ECO:0000305"
FT CONFLICT 608
FT /note="L -> Q (in Ref. 1; AAQ05765)"
FT /evidence="ECO:0000305"
FT CONFLICT 630
FT /note="D -> G (in Ref. 4; BAF84401)"
FT /evidence="ECO:0000305"
FT CONFLICT 758
FT /note="V -> L (in Ref. 1; AAQ05765)"
FT /evidence="ECO:0000305"
FT STRAND 359..364
FT /evidence="ECO:0007829|PDB:2COF"
FT STRAND 367..375
FT /evidence="ECO:0007829|PDB:2COF"
FT STRAND 380..383
FT /evidence="ECO:0007829|PDB:2COF"
FT STRAND 390..396
FT /evidence="ECO:0007829|PDB:2COF"
FT TURN 398..400
FT /evidence="ECO:0007829|PDB:2COF"
FT STRAND 402..404
FT /evidence="ECO:0007829|PDB:2COF"
FT STRAND 414..419
FT /evidence="ECO:0007829|PDB:2COF"
FT STRAND 422..428
FT /evidence="ECO:0007829|PDB:2COF"
FT HELIX 432..445
FT /evidence="ECO:0007829|PDB:2COF"
SQ SEQUENCE 818 AA; 91300 MW; 36040D6D09491DA8 CRC64;
MERYKALEQL LTELDDFLKI LDQENLSSTA LVKKSCLAEL LRLYTKSSSS DEEYIYMNKV
TINKQQNAES QGKAPEEQGL LPNGEPSQHS SAPQKSLPDL PPPKMIPERK QLAIPKTESP
EGYYEEAEPY DTSLNEDGEA VSSSYESYDE EDGSKGKSAP YQWPSPEAGI ELMRDARICA
FLWRKKWLGQ WAKQLCVIKD NRLLCYKSSK DHSPQLDVNL LGSSVIHKEK QVRKKEHKLK
ITPMNADVIV LGLQSKDQAE QWLRVIQEVS GLPSEGASEG NQYTPDAQRF NCQKPDIAEK
YLSASEYGSS VDGHPEVPET KDVKKKCSAG LKLSNLMNLG RKKSTSLEPV ERSLETSSYL
NVLVNSQWKS RWCSVRDNHL HFYQDRNRSK VAQQPLSLVG CEVVPDPSPD HLYSFRILHK
GEELAKLEAK SSEEMGHWLG LLLSESGSKT DPEEFTYDYV DADRVSCIVS AAKNSLLLMQ
RKFSEPNTYI DGLPSQDRQE ELYDDVDLSE LTAAVEPTEE ATPVADDPNE RESDRVYLDL
TPVKSFLHGP SSAQAQASSP TLSCLDNATE ALPADSGPGP TPDEPCIKCP ENLGEQQLES
LEPEDPSLRI TTVKIQTEQQ RISFPPSCPD AVVATPPGAS PPVKDRLRVT SAEIKLGKNR
TEAEVKRYTE EKERLEKKKE EIRGHLAQLR KEKRELKETL LKCTDKEVLA SLEQKLKEID
EECRGEESRR VDLELSIMEV KDNLKKAEAG PVTLGTTVDT THLENVSPRP KAVTPASAPD
CTPVNSATTL KNRPLSVVVT GKGTVLQKAK EWEKKGAS
