BORG4_HUMAN
ID BORG4_HUMAN Reviewed; 356 AA.
AC Q9H3Q1; B3KUS7; O95828; Q96FT3;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Cdc42 effector protein 4;
DE AltName: Full=Binder of Rho GTPases 4;
GN Name=CDC42EP4; Synonyms=BORG4, CEP4;
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).
RC TISSUE=Ileal mucosa;
RX PubMed=11185749; DOI=10.1007/s100380070012;
RA Osada N., Kusuda J., Suzuki Y., Sugano S., Hashimoto K.;
RT "Sequence analysis, gene expression, and chromosomal assignment of mouse
RT Borg4 gene and its human orthologue.";
RL J. Hum. Genet. 45:374-377(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND CHARACTERIZATION.
RC TISSUE=Eye;
RX PubMed=11035016; DOI=10.1074/jbc.m007039200;
RA Hirsch D.S., Pirone D.M., Burbelo P.D.;
RT "A new family of Cdc42 effector proteins, CEPs, function in fibroblast and
RT epithelial cell shape changes.";
RL J. Biol. Chem. 276:875-883(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-174; SER-292 AND SER-295, AND
RP IDENTIFICATION BY 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64; SER-138; SER-174; SER-292
RP AND SER-295, 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64; SER-118; SER-140;
RP SER-142; SER-174 AND SER-295, 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64; SER-105; SER-109;
RP SER-118; SER-138 AND SER-142, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64 AND SER-174, AND
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 [13]
RP METHYLATION [LARGE SCALE ANALYSIS] AT LYS-5, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Probably involved in the organization of the actin
CC cytoskeleton. May act downstream of CDC42 to induce actin filament
CC assembly leading to cell shape changes. Induces pseudopodia formation,
CC when overexpressed in fibroblasts.
CC -!- SUBUNIT: Interacts with CDC42 and RHOQ, in a GTP-dependent manner.
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q9H3Q1; Q8IZU0: FAM9B; NbExp=5; IntAct=EBI-744665, EBI-10175124;
CC Q9H3Q1; P42858: HTT; NbExp=3; IntAct=EBI-744665, EBI-466029;
CC -!- SUBCELLULAR LOCATION: Endomembrane system; Peripheral membrane protein.
CC Cytoplasm, cytoskeleton.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9H3Q1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H3Q1-2; Sequence=VSP_055544;
CC -!- TISSUE SPECIFICITY: Not detected in any of the adult tissues tested.
CC May be expressed only in fetal or embryonic tissues.
CC -!- SIMILARITY: Belongs to the BORG/CEP family. {ECO:0000305}.
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DR EMBL; AB042237; BAB17272.1; -; mRNA.
DR EMBL; AF099664; AAD16299.1; -; mRNA.
DR EMBL; AK097835; BAG53539.1; -; mRNA.
DR EMBL; AC087301; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002774; AAH02774.1; -; mRNA.
DR EMBL; BC010451; AAH10451.1; -; mRNA.
DR CCDS; CCDS11695.1; -. [Q9H3Q1-1]
DR RefSeq; NP_036253.2; NM_012121.4. [Q9H3Q1-1]
DR RefSeq; XP_005257239.1; XM_005257182.2. [Q9H3Q1-1]
DR AlphaFoldDB; Q9H3Q1; -.
DR BioGRID; 117115; 85.
DR IntAct; Q9H3Q1; 32.
DR MINT; Q9H3Q1; -.
DR STRING; 9606.ENSP00000338258; -.
DR iPTMnet; Q9H3Q1; -.
DR PhosphoSitePlus; Q9H3Q1; -.
DR BioMuta; CDC42EP4; -.
DR DMDM; 21362403; -.
DR EPD; Q9H3Q1; -.
DR jPOST; Q9H3Q1; -.
DR MassIVE; Q9H3Q1; -.
DR MaxQB; Q9H3Q1; -.
DR PaxDb; Q9H3Q1; -.
DR PeptideAtlas; Q9H3Q1; -.
DR PRIDE; Q9H3Q1; -.
DR ProteomicsDB; 3730; -.
DR ProteomicsDB; 80739; -. [Q9H3Q1-1]
DR Antibodypedia; 31920; 164 antibodies from 29 providers.
DR DNASU; 23580; -.
DR Ensembl; ENST00000335793.4; ENSP00000338258.3; ENSG00000179604.10. [Q9H3Q1-1]
DR Ensembl; ENST00000439510.2; ENSP00000404270.2; ENSG00000179604.10. [Q9H3Q1-2]
DR GeneID; 23580; -.
DR KEGG; hsa:23580; -.
DR MANE-Select; ENST00000335793.4; ENSP00000338258.3; NM_012121.5; NP_036253.2.
DR UCSC; uc002jjo.4; human. [Q9H3Q1-1]
DR CTD; 23580; -.
DR DisGeNET; 23580; -.
DR GeneCards; CDC42EP4; -.
DR HGNC; HGNC:17147; CDC42EP4.
DR HPA; ENSG00000179604; Low tissue specificity.
DR MIM; 605468; gene.
DR neXtProt; NX_Q9H3Q1; -.
DR OpenTargets; ENSG00000179604; -.
DR PharmGKB; PA38439; -.
DR VEuPathDB; HostDB:ENSG00000179604; -.
DR eggNOG; ENOG502QRD6; Eukaryota.
DR GeneTree; ENSGT00940000161435; -.
DR HOGENOM; CLU_067835_0_0_1; -.
DR InParanoid; Q9H3Q1; -.
DR OMA; HAESMMS; -.
DR PhylomeDB; Q9H3Q1; -.
DR TreeFam; TF331725; -.
DR PathwayCommons; Q9H3Q1; -.
DR Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR Reactome; R-HSA-9013404; RAC2 GTPase cycle.
DR Reactome; R-HSA-9013406; RHOQ GTPase cycle.
DR SignaLink; Q9H3Q1; -.
DR SIGNOR; Q9H3Q1; -.
DR BioGRID-ORCS; 23580; 16 hits in 1077 CRISPR screens.
DR ChiTaRS; CDC42EP4; human.
DR GeneWiki; CDC42EP4; -.
DR GenomeRNAi; 23580; -.
DR Pharos; Q9H3Q1; Tdark.
DR PRO; PR:Q9H3Q1; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9H3Q1; protein.
DR Bgee; ENSG00000179604; Expressed in cranial nerve II and 209 other tissues.
DR ExpressionAtlas; Q9H3Q1; baseline and differential.
DR Genevisible; Q9H3Q1; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:HPA.
DR GO; GO:0005912; C:adherens junction; IDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
DR GO; GO:0045335; C:phagocytic vesicle; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; NAS:UniProtKB.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IEA:Ensembl.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IBA:GO_Central.
DR GO; GO:0031274; P:positive regulation of pseudopodium assembly; IDA:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; IDA:UniProtKB.
DR GO; GO:0007266; P:Rho protein signal transduction; IBA:GO_Central.
DR InterPro; IPR029273; Cdc42_effect.
DR InterPro; IPR000095; CRIB_dom.
DR Pfam; PF14957; BORG_CEP; 1.
DR Pfam; PF00786; PBD; 1.
DR SMART; SM00285; PBD; 1.
DR PROSITE; PS50108; CRIB; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell shape; Cytoplasm; Cytoskeleton; Membrane;
KW Methylation; Phosphoprotein; Reference proteome.
FT CHAIN 1..356
FT /note="Cdc42 effector protein 4"
FT /id="PRO_0000212655"
FT DOMAIN 27..41
FT /note="CRIB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00057"
FT REGION 51..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 122..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 257..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..162
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..318
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..344
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 5
FT /note="N6-methyllysine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JM96"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 105
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 109
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 174
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 292
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231"
FT VAR_SEQ 57..126
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055544"
FT CONFLICT 2
FT /note="P -> L (in Ref. 5; AAH10451)"
FT /evidence="ECO:0000305"
FT CONFLICT 33
FT /note="D -> T (in Ref. 2; AAD16299)"
FT /evidence="ECO:0000305"
FT CONFLICT 288
FT /note="A -> T (in Ref. 2; AAD16299)"
FT /evidence="ECO:0000305"
FT CONFLICT 296
FT /note="A -> T (in Ref. 2; AAD16299)"
FT /evidence="ECO:0000305"
FT CONFLICT 339
FT /note="P -> PP (in Ref. 2; AAD16299)"
FT /evidence="ECO:0000305"
FT CONFLICT 355
FT /note="Missing (in Ref. 2; AAD16299)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 356 AA; 37980 MW; 2CF677C60C6EF1B5 CRC64;
MPILKQLVSS SVHSKRRSRA DLTAEMISAP LGDFRHTMHV GRAGDAFGDT SFLNSKAGEP
DGESLDEQPS SSSSKRSLLS RKFRGSKRSQ SVTRGEREQR DMLGSLRDSA LFVKNAMSLP
QLNEKEAAEK GTSKLPKSLS SSPVKKANDG EGGDEEAGTE EAVPRRNGAA GPHSPDPLLD
EQAFGDLTDL PVVPKATYGL KHAESIMSFH IDLGPSMLGD VLSIMDKEEW DPEEGEGGYH
GDEGAAGTIT QAPPYAVAAP PLARQEGKAG PDLPSLPSHA LEDEGWAAAA PSPGSARSMG
SHTTRDSSSL SSCTSGILEE RSPAFRGPDR ARAAVSRQPD KEFSFMDEEE EDEIRV
