CASS4_HUMAN
ID CASS4_HUMAN Reviewed; 786 AA.
AC Q9NQ75; E1P5Z8; Q5QPD6; Q96K09; Q9BYL5;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Cas scaffolding protein family member 4;
DE AltName: Full=HEF-like protein;
DE AltName: Full=HEF1-EFS-p130Cas-like protein;
DE Short=HEPL;
GN Name=CASS4; Synonyms=C20orf32, HEFL;
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 Jahn T., Will T., Bresolin G., Coutinho S., Peschel C., Duyster J.;
RT "HEF-like protein (HEFL) is involved in integrin signalling.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT SER-660.
RC TISSUE=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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [4]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200; SER-249 AND SER-305, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [7]
RP FUNCTION, INTERACTION WITH PTK2/FAK1, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND PHOSPHORYLATION BY SRC.
RX PubMed=18256281; DOI=10.1091/mbc.e07-09-0953;
RA Singh M.K., Dadke D., Nicolas E., Serebriiskii I.G., Apostolou S.,
RA Canutescu A., Egleston B.L., Golemis E.A.;
RT "A novel Cas family member, HEPL, regulates FAK and cell spreading.";
RL Mol. Biol. Cell 19:1627-1636(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200; SER-249; SER-305;
RP SER-376 AND SER-390, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=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 [9]
RP STRUCTURE BY NMR OF 14-71.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of RSGI RUH-036, an SH3 domain from human.";
RL Submitted (NOV-2005) to the PDB data bank.
CC -!- FUNCTION: Docking protein that plays a role in tyrosine kinase-based
CC signaling related to cell adhesion and cell spreading. Regulates
CC PTK2/FAK1 activity, focal adhesion integrity, and cell spreading.
CC {ECO:0000269|PubMed:18256281}.
CC -!- SUBUNIT: Interacts (via SH3 domain) with PTK2/FAK1 (via C-terminus).
CC {ECO:0000269|PubMed:18256281}.
CC -!- INTERACTION:
CC Q9NQ75-2; Q7Z6G8-3: ANKS1B; NbExp=3; IntAct=EBI-12270182, EBI-17714371;
CC Q9NQ75-2; O14613: CDC42EP2; NbExp=4; IntAct=EBI-12270182, EBI-3438291;
CC Q9NQ75-2; Q13643: FHL3; NbExp=5; IntAct=EBI-12270182, EBI-741101;
CC Q9NQ75-2; Q08379: GOLGA2; NbExp=3; IntAct=EBI-12270182, EBI-618309;
CC Q9NQ75-2; O75031: HSF2BP; NbExp=3; IntAct=EBI-12270182, EBI-7116203;
CC Q9NQ75-2; Q8TDZ2: MICAL1; NbExp=2; IntAct=EBI-12270182, EBI-7153876;
CC Q9NQ75-2; Q15942: ZYX; NbExp=4; IntAct=EBI-12270182, EBI-444225;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:18256281}. Cell junction, focal adhesion
CC {ECO:0000269|PubMed:18256281}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Experimental confirmation may be lacking for some isoforms.;
CC Name=1;
CC IsoId=Q9NQ75-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NQ75-2; Sequence=VSP_003807;
CC Name=3;
CC IsoId=Q9NQ75-3; Sequence=VSP_003806;
CC -!- TISSUE SPECIFICITY: Expressed abundantly in lung and spleen. Also
CC highly expressed in ovarian and leukemia cell lines.
CC {ECO:0000269|PubMed:18256281}.
CC -!- PTM: Phosphorylated on tyrosines by SRC. {ECO:0000269|PubMed:18256281}.
CC -!- SIMILARITY: Belongs to the CAS family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC00655.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ276678; CAC00655.1; ALT_FRAME; mRNA.
DR EMBL; AK027760; BAB55351.1; -; mRNA.
DR EMBL; AL121914; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471077; EAW75546.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75547.1; -; Genomic_DNA.
DR EMBL; BC027951; AAH27951.1; -; mRNA.
DR CCDS; CCDS33492.1; -. [Q9NQ75-1]
DR CCDS; CCDS54475.1; -. [Q9NQ75-3]
DR RefSeq; NP_001157586.1; NM_001164114.1.
DR RefSeq; NP_001157587.1; NM_001164115.1. [Q9NQ75-3]
DR RefSeq; NP_001157588.1; NM_001164116.1. [Q9NQ75-1]
DR RefSeq; NP_065089.2; NM_020356.3. [Q9NQ75-1]
DR PDB; 2CRE; NMR; -; A=14-71.
DR PDBsum; 2CRE; -.
DR AlphaFoldDB; Q9NQ75; -.
DR SMR; Q9NQ75; -.
DR BioGRID; 121359; 8.
DR IntAct; Q9NQ75; 37.
DR STRING; 9606.ENSP00000353462; -.
DR GlyGen; Q9NQ75; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NQ75; -.
DR PhosphoSitePlus; Q9NQ75; -.
DR BioMuta; CASS4; -.
DR DMDM; 23813906; -.
DR EPD; Q9NQ75; -.
DR MassIVE; Q9NQ75; -.
DR MaxQB; Q9NQ75; -.
DR PaxDb; Q9NQ75; -.
DR PeptideAtlas; Q9NQ75; -.
DR PRIDE; Q9NQ75; -.
DR ProteomicsDB; 82093; -. [Q9NQ75-1]
DR ProteomicsDB; 82094; -. [Q9NQ75-2]
DR ProteomicsDB; 82095; -. [Q9NQ75-3]
DR ABCD; Q9NQ75; 2 sequenced antibodies.
DR Antibodypedia; 2766; 76 antibodies from 19 providers.
DR DNASU; 57091; -.
DR Ensembl; ENST00000360314.7; ENSP00000353462.3; ENSG00000087589.17. [Q9NQ75-1]
DR Ensembl; ENST00000434344.2; ENSP00000410027.1; ENSG00000087589.17. [Q9NQ75-3]
DR Ensembl; ENST00000679887.1; ENSP00000506506.1; ENSG00000087589.17. [Q9NQ75-1]
DR GeneID; 57091; -.
DR KEGG; hsa:57091; -.
DR MANE-Select; ENST00000679887.1; ENSP00000506506.1; NM_020356.4; NP_065089.2.
DR UCSC; uc002xxp.3; human. [Q9NQ75-1]
DR CTD; 57091; -.
DR DisGeNET; 57091; -.
DR GeneCards; CASS4; -.
DR HGNC; HGNC:15878; CASS4.
DR HPA; ENSG00000087589; Tissue enhanced (lung, lymphoid tissue).
DR MIM; 618888; gene.
DR neXtProt; NX_Q9NQ75; -.
DR NIAGADS; ENSG00000087589; -.
DR OpenTargets; ENSG00000087589; -.
DR PharmGKB; PA162381095; -.
DR VEuPathDB; HostDB:ENSG00000087589; -.
DR eggNOG; ENOG502QUJM; Eukaryota.
DR GeneTree; ENSGT00950000183008; -.
DR HOGENOM; CLU_017000_0_1_1; -.
DR InParanoid; Q9NQ75; -.
DR OMA; RFASMVI; -.
DR PhylomeDB; Q9NQ75; -.
DR TreeFam; TF328782; -.
DR PathwayCommons; Q9NQ75; -.
DR SignaLink; Q9NQ75; -.
DR BioGRID-ORCS; 57091; 16 hits in 1073 CRISPR screens.
DR ChiTaRS; CASS4; human.
DR EvolutionaryTrace; Q9NQ75; -.
DR GenomeRNAi; 57091; -.
DR Pharos; Q9NQ75; Tbio.
DR PRO; PR:Q9NQ75; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q9NQ75; protein.
DR Bgee; ENSG00000087589; Expressed in upper lobe of left lung and 95 other tissues.
DR ExpressionAtlas; Q9NQ75; baseline and differential.
DR Genevisible; Q9NQ75; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:ARUK-UCL.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
DR GO; GO:1990782; F:protein tyrosine kinase binding; IPI:UniProtKB.
DR GO; GO:0090527; P:actin filament reorganization; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0030335; P:positive regulation of cell migration; IMP:UniProtKB.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IMP:ARUK-UCL.
DR GO; GO:0061098; P:positive regulation of protein tyrosine kinase activity; IDA:UniProtKB.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IMP:UniProtKB.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR CDD; cd12000; SH3_CASS4; 1.
DR Gene3D; 1.20.120.830; -; 1.
DR InterPro; IPR021901; CAS_C.
DR InterPro; IPR037362; CAS_fam.
DR InterPro; IPR035512; CASS4.
DR InterPro; IPR035744; CASS4_SH3.
DR InterPro; IPR014928; Serine_rich_dom.
DR InterPro; IPR038319; Serine_rich_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR10654; PTHR10654; 1.
DR PANTHER; PTHR10654:SF19; PTHR10654:SF19; 1.
DR Pfam; PF12026; CAS_C; 1.
DR Pfam; PF08824; Serine_rich; 1.
DR Pfam; PF14604; SH3_9; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell adhesion; Cell junction;
KW Cytoplasm; Cytoskeleton; Phosphoprotein; Reference proteome; SH3 domain.
FT CHAIN 1..786
FT /note="Cas scaffolding protein family member 4"
FT /id="PRO_0000079425"
FT DOMAIN 11..73
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 262..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 612..670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 612..642
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18088087,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 249
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18088087,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 305
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18088087,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 376
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 390
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 215..651
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_003806"
FT VAR_SEQ 652..786
FT /note="NPGPLIPQPSSQQTPERKPRLSEHCRLYFGALFKAISAFHGSLSSSQPAEII
FT TQSKLVIMVGQKLVDTLCMETQERDVRNEILRGSSHLCSLLKDVALATKNAVLTYPSPA
FT ALGHLQAEAEKLEQHTRQFRGTLG -> VSSEFQVIEKGASIVTWSSGY (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_003807"
FT VARIANT 491
FT /note="R -> K (in dbSNP:rs16979936)"
FT /id="VAR_054084"
FT VARIANT 629
FT /note="T -> N (in dbSNP:rs6069755)"
FT /id="VAR_054085"
FT VARIANT 660
FT /note="P -> S (in dbSNP:rs35031530)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_054086"
FT VARIANT 780
FT /note="Q -> H (in dbSNP:rs7272702)"
FT /id="VAR_054087"
FT CONFLICT 329
FT /note="Y -> N (in Ref. 1; CAC00655)"
FT /evidence="ECO:0000305"
FT CONFLICT 350
FT /note="Missing (in Ref. 1; CAC00655)"
FT /evidence="ECO:0000305"
FT CONFLICT 488
FT /note="E -> A (in Ref. 1; CAC00655)"
FT /evidence="ECO:0000305"
FT STRAND 14..20
FT /evidence="ECO:0007829|PDB:2CRE"
FT STRAND 25..29
FT /evidence="ECO:0007829|PDB:2CRE"
FT STRAND 38..43
FT /evidence="ECO:0007829|PDB:2CRE"
FT STRAND 51..58
FT /evidence="ECO:0007829|PDB:2CRE"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:2CRE"
FT TURN 65..67
FT /evidence="ECO:0007829|PDB:2CRE"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:2CRE"
SQ SEQUENCE 786 AA; 87144 MW; 0E84CD7F60A361DB CRC64;
MKGTGIMDCA PKALLARALY DNCPDCSDEL AFSRGDILTI LEQHVPESEG WWKCLLHGRQ
GLAPANRLQI LTEVAADRPC PPFLRGLEEA PASSEETYQV PTLPRPPTPG PVYEQMRSWA
EGPQPPTAQV YEFPDPPTSA RIICEKTLSF PKQAILTLPR PVRASLPTLP SQVYDVPTQH
RGPVVLKEPE KQQLYDIPAS PKKAGLHPPD SQASGQGVPL ISVTTLRRGG YSTLPNPQKS
EWIYDTPVSP GKASVRNTPL TSFAEESRPH ALPSSSSTFY NPPSGRSRSL TPQLNNNVPM
QKKLSLPEIP SYGFLVPRGT FPLDEDVSYK VPSSFLIPRV EQQNTKPNIY DIPKATSSVS
QAGKELEKAK EVSENSAGHN SSWFSRRTTS PSPEPDRLSG SSSDSRASIV SSCSTTSTDD
SSSSSSEESA KELSLDLDVA KETVMALQHK VVSSVAGLML FVSRKWRFRD YLEANIDAIH
RSTDHIEESV REFLDFARGV HGTACNLTDS NLQNRIRDQM QTISNSYRIL LETKESLDNR
NWPLEVLVTD SVQNSPDDLE RFVMVARMLP EDIKRFASIV IANGRLLFKR NCEKEETVQL
TPNAEFKCEK YIQPPQRETE SHQKSTPSTK QREDEHSSEL LKKNRANICG QNPGPLIPQP
SSQQTPERKP RLSEHCRLYF GALFKAISAF HGSLSSSQPA EIITQSKLVI MVGQKLVDTL
CMETQERDVR NEILRGSSHL CSLLKDVALA TKNAVLTYPS PAALGHLQAE AEKLEQHTRQ
FRGTLG
