TRAF4_MOUSE
ID TRAF4_MOUSE Reviewed; 470 AA.
AC Q61382; Q8BHD9;
DT 09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=TNF receptor-associated factor 4;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q9BUZ4};
DE AltName: Full=Cysteine-rich motif associated to RING and Traf domains protein 1;
GN Name=Traf4; Synonyms=Cart1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Embryonic stem cell;
RX PubMed=9507120; DOI=10.1016/s0925-4773(97)00192-5;
RA Masson R., Regnier C.H., Chenard M.-P., Wendling C., Mattei M.-G.,
RA Tomasetto C., Rio M.-C.;
RT "Tumor necrosis factor receptor associated factor 4 (TRAF4) expression
RT pattern during mouse development.";
RL Mech. Dev. 71:187-191(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Fetus, and Spleen;
RX PubMed=11275257; DOI=10.1016/s0161-5890(00)00098-5;
RA Grech A., Quinn R., Srinivasan D., Badoux X., Brink R.;
RT "Complete structural characterisation of the mammalian and Drosophila TRAF
RT genes: implications for TRAF evolution and the role of RING finger splice
RT variants.";
RL Mol. Immunol. 37:721-734(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Aorta, Embryo, Eye, and Vein;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP POTENTIAL FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=10934170; DOI=10.1016/s0002-9440(10)64578-6;
RA Shiels H., Li X., Schumacker P.T., Maltepe E., Padrid P.A., Sperling A.,
RA Thompson C.B., Lindsten T.;
RT "TRAF4 deficiency leads to tracheal malformation with resulting alterations
RT in air flow to the lungs.";
RL Am. J. Pathol. 157:679-688(2000).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=11943846; DOI=10.1073/pnas.052124799;
RA Regnier C.H., Masson R., Kedinger V., Textoris J., Stoll I., Chenard M.P.,
RA Dierich A., Tomasetto C., Rio M.C.;
RT "Impaired neural tube closure, axial skeleton malformations, and tracheal
RT ring disruption in TRAF4-deficient mice.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:5585-5590(2002).
RN [8]
RP INTERACTION WITH MAP3K4.
RX PubMed=16157600; DOI=10.1074/jbc.c500260200;
RA Abell A.N., Johnson G.L.;
RT "MEKK4 is an effector of the embryonic TRAF4 for JNK activation.";
RL J. Biol. Chem. 280:35793-35796(2005).
RN [9]
RP DISRUPTION PHENOTYPE.
RX PubMed=18284467; DOI=10.1111/j.1365-2567.2008.02810.x;
RA Cherfils-Vicini J., Vingert B., Varin A., Tartour E., Fridman W.H.,
RA Sautes-Fridman C., Regnier C.H., Cremer I.;
RT "Characterization of immune functions in TRAF4-deficient mice.";
RL Immunology 124:562-574(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-426, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Adapter protein with E3 ligase activity that is involved in
CC many diverse biological processes including cell proliferation,
CC migration, differentiation, DNA repair, platelet activation or
CC apoptosis. Promotes EGFR-mediated signaling by facilitating the
CC dimerization of EGFR and downstream AKT activation thereby promoting
CC cell proliferation. Ubiquitinates SMURF2 through 'Lys-48'-linked
CC ubiquitin chain leading to SMURF2 degradation through the proteasome
CC and subsequently osteogenic differentiation. Promotes 'Lys-63'-mediated
CC ubiquitination of CHK1 which in turn activates cell cycle arrest and
CC activation of DNA repair. In addition, promotes an atypical 'Lys-29'-
CC linked ubiquitination at the C-terminal end of IRS1 which is crucial
CC for insulin-like growth factor (IGF) signal transduction (By
CC similarity). Regulates activation of NF-kappa-B in response to
CC signaling through Toll-like receptors. Required for normal skeleton
CC development, and for normal development of the respiratory tract.
CC Required for activation of RPS6KB1 in response to TNF signaling.
CC Modulates TRAF6 functions. Inhibits adipogenic differentiation by
CC activating pyruvate kinase PKM activity and subsequently the beta-
CC catenin signaling pathway (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:Q9BUZ4}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q9BUZ4};
CC -!- PATHWAY: Protein degradation; proteasomal ubiquitin-dependent pathway.
CC {ECO:0000250|UniProtKB:Q9BUZ4}.
CC -!- SUBUNIT: Homotrimer. Interacts with LTBR/TNFRSF3, NGFR/TNFRSF16,
CC RPS6KB1 and TGFB1I1. Interacts with SMURF1. Interacts (via TRAF domain)
CC with MAP3K4 (via kinase domain). Interacts with NCF1, TICAM1, IRAK1 and
CC TRAF6, and is probably part of a complex containing TRAF4, NCF1,
CC TICAM1, IRAK1 and TRAF6. Interacts (via MATH domain) with GP6 and
CC GP1BB. Interacts with EGFR (via C-terminal region); this interaction
CC promotes the formation of EGFR asymmetric dimers. Interacts with PKM;
CC this interaction promotes PKM kinase activity.
CC {ECO:0000250|UniProtKB:Q9BUZ4}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9BUZ4}. Nucleus
CC {ECO:0000250|UniProtKB:Q9BUZ4}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:Q9BUZ4}. Cell junction, tight junction
CC {ECO:0000250|UniProtKB:Q9BUZ4}. Cell membrane
CC {ECO:0000250|UniProtKB:Q9BUZ4}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9BUZ4}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q9BUZ4}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q9BUZ4}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in brain. Preferentially
CC expressed by postmitotic undifferentiated neurons in developing central
CC (CNS) and peripheral (PNS) nervous system, and in nervous tissues of
CC sensory organs. In the embryo, protein expression was shown in brain,
CC thymus, salivary glands and intestine. In the adult, protein expression
CC is restricted to the brain (hippocampus and olfactory bulb).
CC {ECO:0000269|PubMed:9507120}.
CC -!- DEVELOPMENTAL STAGE: Strongly expressed throughout embryogenesis with a
CC maximum from 8.5 to 13.5 dpc. {ECO:0000269|PubMed:9507120}.
CC -!- DOMAIN: The coiled coil domain mediates homo- and hetero-
CC oligomerization. {ECO:0000250}.
CC -!- DOMAIN: The MATH/TRAF domain binds to receptor cytoplasmic domains.
CC {ECO:0000250}.
CC -!- PTM: Polyubiquitinated, leading to its proteasomal degradation.
CC {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mice exhibit considerable phenotypic variability,
CC depending in part on the strain. In one strain pups are born at the
CC expected Mendelian frequency, while in another strain up to one third
CC die during embryogenesis. Mutants that reach adulthood are fertile, but
CC have on average three pups per litter instead of ten in wild-type.
CC Mutants have an apparently normal immune response, with no defects in
CC the development of T and B-lymphocytes, granulocytes, macrophages and
CC dendritic cells. Mutants have respiratory problems, due to
CC developmental defects of the trachea, stem bronchi and rib cage. They
CC exhibit severe skeletal alterations at the level of the spinal column,
CC including scoliosis and kyphosis, and have curly tails. Many also
CC display neural tube closure defects. {ECO:0000269|PubMed:10934170,
CC ECO:0000269|PubMed:11943846, ECO:0000269|PubMed:18284467}.
CC -!- SIMILARITY: Belongs to the TNF receptor-associated factor family. B
CC subfamily. {ECO:0000305}.
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DR EMBL; X92346; CAA63103.1; -; mRNA.
DR EMBL; AF233449; AAF44757.1; -; mRNA.
DR EMBL; AK035056; BAC28928.1; -; mRNA.
DR EMBL; AK040877; BAC30729.1; -; mRNA.
DR EMBL; AK053900; BAC35582.1; -; mRNA.
DR EMBL; AL591070; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466596; EDL12913.1; -; Genomic_DNA.
DR CCDS; CCDS25090.1; -.
DR RefSeq; NP_033449.2; NM_009423.4.
DR AlphaFoldDB; Q61382; -.
DR SMR; Q61382; -.
DR BioGRID; 204305; 7.
DR STRING; 10090.ENSMUSP00000017530; -.
DR iPTMnet; Q61382; -.
DR PhosphoSitePlus; Q61382; -.
DR EPD; Q61382; -.
DR jPOST; Q61382; -.
DR MaxQB; Q61382; -.
DR PaxDb; Q61382; -.
DR PeptideAtlas; Q61382; -.
DR PRIDE; Q61382; -.
DR ProteomicsDB; 258962; -.
DR Antibodypedia; 3961; 324 antibodies from 39 providers.
DR DNASU; 22032; -.
DR Ensembl; ENSMUST00000017530; ENSMUSP00000017530; ENSMUSG00000017386.
DR GeneID; 22032; -.
DR KEGG; mmu:22032; -.
DR UCSC; uc007kif.2; mouse.
DR CTD; 9618; -.
DR MGI; MGI:1202880; Traf4.
DR VEuPathDB; HostDB:ENSMUSG00000017386; -.
DR eggNOG; KOG0297; Eukaryota.
DR GeneTree; ENSGT00940000158628; -.
DR HOGENOM; CLU_021061_6_0_1; -.
DR InParanoid; Q61382; -.
DR OMA; MKQLQSH; -.
DR OrthoDB; 918518at2759; -.
DR PhylomeDB; Q61382; -.
DR TreeFam; TF321154; -.
DR UniPathway; UPA00144; -.
DR BioGRID-ORCS; 22032; 0 hits in 75 CRISPR screens.
DR ChiTaRS; Traf4; mouse.
DR PRO; PR:Q61382; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q61382; protein.
DR Bgee; ENSMUSG00000017386; Expressed in cortical plate and 214 other tissues.
DR Genevisible; Q61382; MM.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0031996; F:thioesterase binding; ISO:MGI.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0005164; F:tumor necrosis factor receptor binding; ISO:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0050699; F:WW domain binding; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007250; P:activation of NF-kappaB-inducing kinase activity; IEA:InterPro.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0046330; P:positive regulation of JNK cascade; ISS:UniProtKB.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; ISS:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
DR GO; GO:0043122; P:regulation of I-kappaB kinase/NF-kappaB signaling; IBA:GO_Central.
DR GO; GO:0007585; P:respiratory gaseous exchange by respiratory system; IMP:MGI.
DR GO; GO:0030323; P:respiratory tube development; IMP:MGI.
DR CDD; cd03781; MATH_TRAF4; 1.
DR Gene3D; 2.60.210.10; -; 1.
DR Gene3D; 3.30.40.10; -; 4.
DR InterPro; IPR002083; MATH/TRAF_dom.
DR InterPro; IPR043211; TNF_rcpt-assoc_TRAF.
DR InterPro; IPR012227; TNF_rcpt-assoc_TRAF_met.
DR InterPro; IPR008974; TRAF-like.
DR InterPro; IPR027138; TRAF4.
DR InterPro; IPR037307; TRAF4_MATH.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR InterPro; IPR001293; Znf_TRAF.
DR PANTHER; PTHR10131; PTHR10131; 2.
DR PANTHER; PTHR10131:SF120; PTHR10131:SF120; 2.
DR Pfam; PF00097; zf-C3HC4; 1.
DR Pfam; PF02176; zf-TRAF; 2.
DR PIRSF; PIRSF015614; TRAF; 1.
DR SMART; SM00061; MATH; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50144; MATH; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS50145; ZF_TRAF; 3.
PE 1: Evidence at protein level;
KW Apoptosis; Cell junction; Cell membrane; Coiled coil; Cytoplasm;
KW Cytoskeleton; Developmental protein; Immunity; Innate immunity; Membrane;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Tight junction; Transferase; Ubl conjugation; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..470
FT /note="TNF receptor-associated factor 4"
FT /id="PRO_0000056404"
FT DOMAIN 307..462
FT /note="MATH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00129"
FT ZN_FING 18..58
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 101..154
FT /note="TRAF-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00207"
FT ZN_FING 155..208
FT /note="TRAF-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00207"
FT ZN_FING 209..267
FT /note="TRAF-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00207"
FT COILED 277..310
FT /evidence="ECO:0000255"
FT MOD_RES 426
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 4
FT /note="F -> L (in Ref. 1; CAA63103)"
FT /evidence="ECO:0000305"
FT CONFLICT 9
FT /note="L -> P (in Ref. 1; CAA63103)"
FT /evidence="ECO:0000305"
FT CONFLICT 27..30
FT /note="EPVQ -> DSVE (in Ref. 1; CAA63103)"
FT /evidence="ECO:0000305"
FT CONFLICT 38
FT /note="F -> Y (in Ref. 1; CAA63103)"
FT /evidence="ECO:0000305"
FT CONFLICT 41
FT /note="T -> N (in Ref. 1; CAA63103)"
FT /evidence="ECO:0000305"
FT CONFLICT 166
FT /note="Y -> F (in Ref. 1; CAA63103)"
FT /evidence="ECO:0000305"
FT CONFLICT 244
FT /note="S -> R (in Ref. 1; CAA63103)"
FT /evidence="ECO:0000305"
FT CONFLICT 351
FT /note="F -> S (in Ref. 1; CAA63103)"
FT /evidence="ECO:0000305"
FT CONFLICT 382
FT /note="F -> L (in Ref. 1; CAA63103)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 470 AA; 53504 MW; 2C99A876E98B99C5 CRC64;
MPGFDYKFLE KPKRRLLCPL CGKPMREPVQ VSTCGHRFCD TCLQEFLSEG VFKCPEDQLP
LDYAKIYPDP ELEVQVLGLA IRCIHSEEGC RWSGPLRHLQ GHLNTCSFNV VPCPNRCPAK
LSRRDLPAHL QHDCPKRRLK CEFCGCDFSG EAYESHEGVC PQESVYCENK CGARMMRRLL
AQHATSECPK RTQPCAYCTK EFVYDTIQSH QYQCPRLPVP CPNQCGVGTV AREDLPTHLK
DSCSTAFVLC PFKESGCKHR CPKLAMGRHV EESVKPHLAM MCALVSRQRQ ELQELRRELE
ELSIGSDGVL IWKIGSYGRR LQEAKAKPNL ECFSPAFYTH KYGYKLQVSA FLNGNGSGEG
THLSIYIRVL PGAFDNLLEW PFARRVTFSL LDQSDPGLAK PQHVTETFHP DPNWKNFQKP
GTWRGSLDES SLGFGYPKFI SHQDIRKRNY VRDDAVFIRA SVELPRKILS
