ID FARP2_HUMAN Reviewed; 1054 AA.
AC O94887; B7Z6J8; F5GZ84; Q53QM5; Q8WU27; Q9UFE7;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 3.
DT 24-JAN-2024, entry version 173.
DE RecName: Full=FERM, ARHGEF and pleckstrin domain-containing protein 2;
DE AltName: Full=FERM domain-including RhoGEF;
DE Short=FIR;
DE AltName: Full=FERM, RhoGEF and pleckstrin domain-containing protein 2;
DE AltName: Full=Pleckstrin homology domain-containing family C member 3;
DE Short=PH domain-containing family C member 3;
GN Name=FARP2; Synonyms=KIAA0793, PLEKHC3;
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] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9872452; DOI=10.1093/dnares/5.5.277;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XI. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:277-286(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 825-1054.
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE 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 [7]
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 [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-389 AND SER-439, AND
RP IDENTIFICATION BY MASS 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: Functions as a guanine nucleotide exchange factor that
CC activates RAC1. May have relatively low activity. Plays a role in the
CC response to class 3 semaphorins and remodeling of the actin
CC cytoskeleton. Plays a role in TNFSF11-mediated osteoclast
CC differentiation, especially in podosome rearrangement and
CC reorganization of the actin cytoskeleton. Regulates the activation of
CC ITGB3, integrin signaling and cell adhesion (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with PLXNA1. Interaction with PLXNA1 or PIP5K1C
CC lowers its guanine nucleotide exchange activity. Dissociates from
CC PLXNA1 when SEMA3A binds to the receptor. Interacts with PIP5K1C via
CC its FERM domain. The interaction with PIP5K1C is enhanced by SEMA3A
CC binding. Interacts with RAC1 (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O94887-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O94887-2; Sequence=VSP_017977, VSP_017978;
CC Name=3;
CC IsoId=O94887-3; Sequence=VSP_054840, VSP_054841;
CC -!- DOMAIN: Intramolecular interaction between the DH domain and the PH
CC domains can stabilize the protein in an autoinhibited conformation.
CC {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA34513.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB018336; BAA34513.2; ALT_INIT; mRNA.
DR EMBL; AK300435; BAH13284.1; -; mRNA.
DR EMBL; AC005104; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC110299; AAY14682.1; -; Genomic_DNA.
DR EMBL; BC021301; AAH21301.1; -; mRNA.
DR EMBL; AL122052; CAB59185.1; -; mRNA.
DR CCDS; CCDS33424.1; -. [O94887-1]
DR CCDS; CCDS63197.1; -. [O94887-2]
DR CCDS; CCDS63198.1; -. [O94887-3]
DR PIR; T34541; T34541.
DR RefSeq; NP_001269912.1; NM_001282983.1. [O94887-2]
DR RefSeq; NP_001269913.1; NM_001282984.1. [O94887-3]
DR RefSeq; NP_055623.1; NM_014808.3. [O94887-1]
DR AlphaFoldDB; O94887; -.
DR SMR; O94887; -.
DR BioGRID; 115189; 91.
DR CORUM; O94887; -.
DR IntAct; O94887; 37.
DR MINT; O94887; -.
DR STRING; 9606.ENSP00000264042; -.
DR iPTMnet; O94887; -.
DR PhosphoSitePlus; O94887; -.
DR SwissPalm; O94887; -.
DR BioMuta; FARP2; -.
DR EPD; O94887; -.
DR jPOST; O94887; -.
DR MassIVE; O94887; -.
DR MaxQB; O94887; -.
DR PaxDb; 9606-ENSP00000264042; -.
DR PeptideAtlas; O94887; -.
DR ProteomicsDB; 24958; -.
DR ProteomicsDB; 50524; -. [O94887-1]
DR ProteomicsDB; 50525; -. [O94887-2]
DR Pumba; O94887; -.
DR Antibodypedia; 34561; 182 antibodies from 23 providers.
DR DNASU; 9855; -.
DR Ensembl; ENST00000264042.8; ENSP00000264042.3; ENSG00000006607.14. [O94887-1]
DR Ensembl; ENST00000373287.8; ENSP00000362384.4; ENSG00000006607.14. [O94887-2]
DR Ensembl; ENST00000627550.2; ENSP00000486597.1; ENSG00000006607.14. [O94887-3]
DR GeneID; 9855; -.
DR KEGG; hsa:9855; -.
DR MANE-Select; ENST00000264042.8; ENSP00000264042.3; NM_014808.4; NP_055623.1.
DR UCSC; uc002wbi.4; human. [O94887-1]
DR AGR; HGNC:16460; -.
DR CTD; 9855; -.
DR DisGeNET; 9855; -.
DR GeneCards; FARP2; -.
DR HGNC; HGNC:16460; FARP2.
DR HPA; ENSG00000006607; Low tissue specificity.
DR MIM; 617586; gene.
DR neXtProt; NX_O94887; -.
DR OpenTargets; ENSG00000006607; -.
DR PharmGKB; PA134873245; -.
DR VEuPathDB; HostDB:ENSG00000006607; -.
DR eggNOG; KOG3531; Eukaryota.
DR GeneTree; ENSGT00940000158642; -.
DR HOGENOM; CLU_012301_0_0_1; -.
DR InParanoid; O94887; -.
DR OMA; HKHMPED; -.
DR OrthoDB; 2876516at2759; -.
DR PhylomeDB; O94887; -.
DR TreeFam; TF351276; -.
DR PathwayCommons; O94887; -.
DR Reactome; R-HSA-399955; SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR SignaLink; O94887; -.
DR SIGNOR; O94887; -.
DR BioGRID-ORCS; 9855; 7 hits in 1153 CRISPR screens.
DR ChiTaRS; FARP2; human.
DR GeneWiki; FARP2; -.
DR GenomeRNAi; 9855; -.
DR Pharos; O94887; Tbio.
DR PRO; PR:O94887; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; O94887; Protein.
DR Bgee; ENSG00000006607; Expressed in colonic epithelium and 175 other cell types or tissues.
DR ExpressionAtlas; O94887; baseline and differential.
DR Genevisible; O94887; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0008092; F:cytoskeletal protein binding; IEA:InterPro.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:MGI.
DR GO; GO:0030036; P:actin cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; ISS:UniProtKB.
DR GO; GO:0022405; P:hair cycle process; IEA:Ensembl.
DR GO; GO:0016322; P:neuron remodeling; IDA:MGI.
DR GO; GO:0030316; P:osteoclast differentiation; ISS:UniProtKB.
DR GO; GO:0071800; P:podosome assembly; ISS:UniProtKB.
DR GO; GO:0016601; P:Rac protein signal transduction; IDA:MGI.
DR GO; GO:0033623; P:regulation of integrin activation; ISS:UniProtKB.
DR GO; GO:0071526; P:semaphorin-plexin signaling pathway; ISS:UniProtKB.
DR CDD; cd14473; FERM_B-lobe; 1.
DR CDD; cd13193; FERM_C_FARP1-like; 1.
DR CDD; cd17190; FERM_F1_FARP2; 1.
DR CDD; cd01220; PH1_FARP1-like; 1.
DR CDD; cd13235; PH2_FARP1-like; 1.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 3.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR000798; Ez/rad/moesin-like.
DR InterPro; IPR014847; FA.
DR InterPro; IPR041788; FARP1/FARP2/FRMD7_FERM_C.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR InterPro; IPR035963; FERM_2.
DR InterPro; IPR019748; FERM_central.
DR InterPro; IPR019747; FERM_CS.
DR InterPro; IPR000299; FERM_domain.
DR InterPro; IPR018979; FERM_N.
DR InterPro; IPR018980; FERM_PH-like_C.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR45858; FERM DOMAIN CONTAINING PROTEIN; 1.
DR PANTHER; PTHR45858:SF4; FERM, ARHGEF AND PLECKSTRIN DOMAIN-CONTAINING PROTEIN 2; 1.
DR Pfam; PF08736; FA; 1.
DR Pfam; PF09380; FERM_C; 1.
DR Pfam; PF00373; FERM_M; 1.
DR Pfam; PF09379; FERM_N; 1.
DR Pfam; PF00169; PH; 2.
DR Pfam; PF00621; RhoGEF; 1.
DR PRINTS; PR00935; BAND41.
DR PRINTS; PR00661; ERMFAMILY.
DR SMART; SM00295; B41; 1.
DR SMART; SM01195; FA; 1.
DR SMART; SM01196; FERM_C; 1.
DR SMART; SM00233; PH; 2.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF50729; PH domain-like; 3.
DR SUPFAM; SSF47031; Second domain of FERM; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS00660; FERM_1; 1.
DR PROSITE; PS50057; FERM_3; 1.
DR PROSITE; PS50003; PH_DOMAIN; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Guanine-nucleotide releasing factor; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..1054
FT /note="FERM, ARHGEF and pleckstrin domain-containing
FT protein 2"
FT /id="PRO_0000232755"
FT DOMAIN 44..324
FT /note="FERM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT DOMAIN 535..726
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 755..852
FT /note="PH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 929..1026
FT /note="PH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 421..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 856..894
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1029..1054
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..435
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 389
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 439
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 632..647
FT /note="EFTSYFQRHDEVLTEL -> VFQLHEGHVAGVTKME (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017977"
FT VAR_SEQ 632..638
FT /note="EFTSYFQ -> AAHEFTT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054840"
FT VAR_SEQ 639..1054
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054841"
FT VAR_SEQ 648..1054
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017978"
FT VARIANT 185
FT /note="K -> N (in dbSNP:rs16843643)"
FT /id="VAR_048363"
FT VARIANT 260
FT /note="T -> I (in dbSNP:rs757978)"
FT /id="VAR_048364"
FT VARIANT 643
FT /note="V -> I (in dbSNP:rs41342147)"
FT /id="VAR_048365"
FT CONFLICT 366
FT /note="E -> G (in Ref. 2; BAH13284)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1054 AA; 119888 MW; 7DC279F69A307E5A CRC64;
MGEIEGTYRV LQTAGMRLGA QTPVGVSTLE PGQTLLPRMQ EKHLHLRVKL LDNTMEIFDI
EPKCDGQVLL TQVWKRLNLV ECDYFGMEFQ NTQSYWIWLE PMKPIIRQIR RPKNVVLRLA
VKFFPPDPGQ LQEEYTRYLF ALQLKRDLLE ERLTCADTTA ALLTSHLLQS EIGDYDETLD
REHLKVNEYL PGQQHCLEKI LEFHQKHVGQ TPAESDFQVL EIARKLEMYG IRFHMASDRE
GTKIQLAVSH MGVLVFQGTT KINTFNWSKV RKLSFKRKRF LIKLHPEVHG PYQDTLEFLL
GSRDECKNFW KICVEYHTFF RLLDQPKPKA KAVFFSRGSS FRYSGRTQKQ LVDYFKDSGM
KRIPYERRHS KTHTSVRALT ADLPKQSISF PEGLRTPASP SSANAFYSLS PSTLVPSGLP
EFKDSSSSLT DPQVSYVKSP AAERRSGAVA GGPDTPSAQP LGPPALQPGP GLSTKSPQPS
PSSRKSPLSL SPAFQVPLGP AEQGSSPLLS PVLSDAGGAG MDCEEPRHKR VPADEAYFIV
KEILATERTY LKDLEVITVW FRSAVVKEDA MPATLMTLLF SNIDPIYEFH RGFLREVEQR
LALWEGPSKA HTKGSHQRIG DILLRNMRQL KEFTSYFQRH DEVLTELEKA TKRCKKLEAV
YKEFELQKVC YLPLNTFLLK PIQRLLHYRL LLRRLCGHYS PGHHDYADCH DALKAITEVT
TTLQHILIRL ENLQKLTELQ RDLVGIENLI APGREFIREG CLHKLTKKGL QQRMFFLFSD
MLLYTSKGVA GTSHFRIRGL LPLQGMLVEE SDNEWSVPHC FTIYAAQKTI VVAASTRLEK
EKWMLDLNSA IQAAKSGGDT APALPGRTVC TRPPRSPNEV SLEQESEDDA RGVRSSLEGH
GQHRANTTMH VCWYRNTSVS RADHSAAVEN QLSGYLLRKF KNSHGWQKLW VVFTNFCLFF
YKTHQDDYPL ASLPLLGYSV SIPREADGIH KDYVFKLQFK SHVYFFRAES KYTFERWMEV
IQGASSSAGR APSIVQDGPQ PSSGLEGMVR GKEE
//
