FMNL3_HUMAN
ID FMNL3_HUMAN Reviewed; 1028 AA.
AC Q8IVF7; B0JZA7; Q6ZRJ1;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 3.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Formin-like protein 3;
DE AltName: Full=Formin homology 2 domain-containing protein 3;
DE AltName: Full=WW domain-binding protein 3;
DE Short=WBP-3;
GN Name=FMNL3; Synonyms=FHOD3, FRL2, KIAA2014, WBP3;
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 3).
RC TISSUE=Brain;
RA Nagase T., Kikuno R., Ohara O.;
RT "The nucleotide sequence of a long cDNA clone isolated from human.";
RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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 IDENTIFICATION (ISOFORMS 1 AND 3).
RX PubMed=12684686;
RA Katoh M., Katoh M.;
RT "Identification and characterization of human FMNL1, FMNL2 and FMNL3 genes
RT in silico.";
RL Int. J. Oncol. 22:1161-1168(2003).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-174, 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 MYRISTOYLATION AT GLY-2.
RX PubMed=20213681; DOI=10.1002/pmic.200900783;
RA Suzuki T., Moriya K., Nagatoshi K., Ota Y., Ezure T., Ando E.,
RA Tsunasawa S., Utsumi T.;
RT "Strategy for comprehensive identification of human N-myristoylated
RT proteins using an insect cell-free protein synthesis system.";
RL Proteomics 10:1780-1793(2010).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21834987; DOI=10.1186/1741-7007-9-54;
RA Bai S.W., Herrera-Abreu M.T., Rohn J.L., Racine V., Tajadura V.,
RA Suryavanshi N., Bechtel S., Wiemann S., Baum B., Ridley A.J.;
RT "Identification and characterization of a set of conserved and new
RT regulators of cytoskeletal organisation, cell morphology and migration.";
RL BMC Biol. 9:54-54(2011).
RN [9]
RP INTERACTION WITH SRGAP2.
RX PubMed=21148482; DOI=10.1074/jbc.m110.190397;
RA Mason F.M., Heimsath E.G., Higgs H.N., Soderling S.H.;
RT "Bi-modal regulation of a formin by srGAP2.";
RL J. Biol. Chem. 286:6577-6586(2011).
RN [10]
RP FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=22275430; DOI=10.1242/jcs.091066;
RA Hetheridge C., Scott A.N., Swain R.K., Copeland J.W., Higgs H.N.,
RA Bicknell R., Mellor H.;
RT "The formin FMNL3 is a cytoskeletal regulator of angiogenesis.";
RL J. Cell Sci. 125:1420-1428(2012).
CC -!- FUNCTION: Plays a role in the regulation of cell morphology and
CC cytoskeletal organization. Required in the control of cell shape and
CC migration. Required for developmental angiogenesis (By similarity). In
CC this process, required for microtubule reorganization and for efficient
CC endothelial cell elongation. In quiescent endothelial cells, triggers
CC rearrangement of the actin cytoskeleton, but does not alter microtubule
CC alignement. {ECO:0000250|UniProtKB:Q6NXC0, ECO:0000269|PubMed:21834987,
CC ECO:0000269|PubMed:22275430}.
CC -!- SUBUNIT: Interacts with SRGAP2 (via SH3 domain).
CC {ECO:0000269|PubMed:21148482}.
CC -!- INTERACTION:
CC Q8IVF7-3; P36639-2: NUDT1; NbExp=3; IntAct=EBI-12414373, EBI-12380931;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21834987}. Cell
CC membrane {ECO:0000269|PubMed:22275430}; Lipid-anchor {ECO:0000255}.
CC Note=Enriched in lamellipodia.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8IVF7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8IVF7-2; Sequence=VSP_025892, VSP_025893;
CC Name=3;
CC IsoId=Q8IVF7-3; Sequence=VSP_025893;
CC -!- TISSUE SPECIFICITY: Expressed in endothelial cells.
CC {ECO:0000269|PubMed:22275430}.
CC -!- DOMAIN: The DAD domain regulates activation via by an autoinhibitory
CC interaction with the GBD/FH3 domain. This autoinhibition is released
CC upon competitive binding of an activated GTPase. The release of DAD
CC allows the FH2 domain to then nucleate and elongate nonbranched actin
CC filaments (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the formin homology family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC23110.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB095934; BAC23110.2; ALT_INIT; mRNA.
DR EMBL; AK128195; BAC87319.1; -; mRNA.
DR EMBL; AC020612; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC159100; AAI59101.1; -; mRNA.
DR CCDS; CCDS41780.1; -. [Q8IVF7-2]
DR CCDS; CCDS44874.1; -. [Q8IVF7-3]
DR RefSeq; NP_783863.4; NM_175736.4. [Q8IVF7-3]
DR RefSeq; NP_944489.2; NM_198900.2. [Q8IVF7-2]
DR RefSeq; XP_005269275.1; XM_005269218.2.
DR AlphaFoldDB; Q8IVF7; -.
DR SMR; Q8IVF7; -.
DR BioGRID; 124787; 31.
DR IntAct; Q8IVF7; 13.
DR MINT; Q8IVF7; -.
DR STRING; 9606.ENSP00000335655; -.
DR iPTMnet; Q8IVF7; -.
DR PhosphoSitePlus; Q8IVF7; -.
DR BioMuta; FMNL3; -.
DR DMDM; 148886617; -.
DR EPD; Q8IVF7; -.
DR jPOST; Q8IVF7; -.
DR MassIVE; Q8IVF7; -.
DR MaxQB; Q8IVF7; -.
DR PaxDb; Q8IVF7; -.
DR PeptideAtlas; Q8IVF7; -.
DR PRIDE; Q8IVF7; -.
DR ProteomicsDB; 70699; -. [Q8IVF7-1]
DR ProteomicsDB; 70700; -. [Q8IVF7-2]
DR ProteomicsDB; 70701; -. [Q8IVF7-3]
DR Antibodypedia; 1106; 77 antibodies from 14 providers.
DR DNASU; 91010; -.
DR Ensembl; ENST00000335154.10; ENSP00000335655.5; ENSG00000161791.14. [Q8IVF7-3]
DR Ensembl; ENST00000352151.9; ENSP00000344311.5; ENSG00000161791.14. [Q8IVF7-2]
DR GeneID; 91010; -.
DR KEGG; hsa:91010; -.
DR MANE-Select; ENST00000335154.10; ENSP00000335655.5; NM_175736.5; NP_783863.4. [Q8IVF7-3]
DR UCSC; uc001ruv.2; human. [Q8IVF7-1]
DR CTD; 91010; -.
DR DisGeNET; 91010; -.
DR GeneCards; FMNL3; -.
DR HGNC; HGNC:23698; FMNL3.
DR HPA; ENSG00000161791; Low tissue specificity.
DR MIM; 616288; gene.
DR neXtProt; NX_Q8IVF7; -.
DR OpenTargets; ENSG00000161791; -.
DR PharmGKB; PA134992328; -.
DR VEuPathDB; HostDB:ENSG00000161791; -.
DR eggNOG; KOG1923; Eukaryota.
DR GeneTree; ENSGT00940000159962; -.
DR HOGENOM; CLU_003597_0_0_1; -.
DR InParanoid; Q8IVF7; -.
DR OMA; ELANFWH; -.
DR OrthoDB; 288325at2759; -.
DR PhylomeDB; Q8IVF7; -.
DR TreeFam; TF325155; -.
DR PathwayCommons; Q8IVF7; -.
DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR Reactome; R-HSA-8980692; RHOA GTPase cycle.
DR Reactome; R-HSA-9013106; RHOC GTPase cycle.
DR Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR Reactome; R-HSA-9013409; RHOJ GTPase cycle.
DR SignaLink; Q8IVF7; -.
DR BioGRID-ORCS; 91010; 15 hits in 1079 CRISPR screens.
DR ChiTaRS; FMNL3; human.
DR GeneWiki; FMNL3; -.
DR GenomeRNAi; 91010; -.
DR Pharos; Q8IVF7; Tbio.
DR PRO; PR:Q8IVF7; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q8IVF7; protein.
DR Bgee; ENSG00000161791; Expressed in sural nerve and 136 other tissues.
DR ExpressionAtlas; Q8IVF7; baseline and differential.
DR Genevisible; Q8IVF7; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0032794; F:GTPase activating protein binding; ISS:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0016477; P:cell migration; IMP:UniProtKB.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0007010; P:cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; IMP:UniProtKB.
DR Gene3D; 1.20.58.2220; -; 1.
DR Gene3D; 1.25.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR015425; FH2_Formin.
DR InterPro; IPR042201; FH2_Formin_sf.
DR InterPro; IPR010472; FH3_dom.
DR InterPro; IPR027655; Fmnl3.
DR InterPro; IPR043592; FMNL_animal.
DR InterPro; IPR014768; GBD/FH3_dom.
DR InterPro; IPR010473; GTPase-bd.
DR PANTHER; PTHR45857; PTHR45857; 1.
DR PANTHER; PTHR45857:SF3; PTHR45857:SF3; 1.
DR Pfam; PF06367; Drf_FH3; 1.
DR Pfam; PF06371; Drf_GBD; 2.
DR Pfam; PF02181; FH2; 1.
DR SMART; SM01139; Drf_FH3; 1.
DR SMART; SM01140; Drf_GBD; 1.
DR SMART; SM00498; FH2; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS51444; FH2; 1.
DR PROSITE; PS51232; GBD_FH3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Angiogenesis; Cell membrane; Cytoplasm;
KW Developmental protein; Lipoprotein; Membrane; Myristate; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..1028
FT /note="Formin-like protein 3"
FT /id="PRO_0000289095"
FT DOMAIN 26..472
FT /note="GBD/FH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00579"
FT DOMAIN 561..951
FT /note="FH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00774"
FT DOMAIN 986..1018
FT /note="DAD"
FT REGION 493..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..541
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 95
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZPF4"
FT MOD_RES 174
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1014
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZPF4"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:20213681"
FT VAR_SEQ 152..202
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_025892"
FT VAR_SEQ 999..1028
FT /note="VLKSVPFTARTAKRGSRFFCDAAHHDESNC -> GLHCQPMVVRHQARSAAP
FT PSGPPRAPGPH (in isoform 3 and isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.1"
FT /id="VSP_025893"
SQ SEQUENCE 1028 AA; 117213 MW; 79A574506A0FD6E1 CRC64;
MGNLESAEGV PGEPPSVPLL LPPGKMPMPE PCELEERFAL VLSSMNLPPD KARLLRQYDN
EKKWDLICDQ ERFQVKNPPH TYIQKLQSFL DPSVTRKKFR RRVQESTKVL RELEISLRTN
HIGWVREFLN DENKGLDVLV DYLSFAQCSV MFDFEGLESG DDGAFDKLRS WSRSIEDLQP
PSALSAPFTN SLARSARQSV LRYSTLPGRR ALKNSRLVSQ KDDVHVCILC LRAIMNYQYG
FNLVMSHPHA VNEIALSLNN KNPRTKALVL ELLAAVCLVR GGHEIILAAF DNFKEVCKEL
HRFEKLMEYF RNEDSNIDFM VACMQFINIV VHSVEDMNFR VHLQYEFTKL GLEEFLQKSR
HTESEKLQVQ IQAYLDNVFD VGGLLEDAET KNVALEKVEE LEEHVSHLTE KLLDLENENM
MRVAELEKQL LQREKELESI KETYENTSHQ VHTLRRLIKE KEEAFQRRCH LEPNVRGLES
VDSEALARVG PAELSEGMPP SDLDLLAPAP PPEEVLPLPP PPAPPLPPPP PPLPDKCPPA
PPLPGAAPSV VLTVGLSAIR IKKPIKTKFR LPVFNWTALK PNQISGTVFS ELDDEKILED
LDLDKFEELF KTKAQGPALD LICSKNKTAQ KAASKVTLLE ANRAKNLAIT LRKAGRSAEE
ICRAIHTFDL QTLPVDFVEC LMRFLPTEAE VKLLRQYERE RQPLEELAAE DRFMLLFSKV
ERLTQRMAGM AFLGNFQDNL QMLTPQLNAI IAASASVKSS QKLKQMLEII LALGNYMNSS
KRGAVYGFKL QSLDLLLDTK STDRKMTLLH FIALTVKEKY PDLANFWHEL HFVEKAAAVS
LENVLLDVKE LGRGMELIRR ECSIHDNSVL RNFLSTNEGK LDKLQRDAKT AEEAYNAVVR
YFGESPKTTP PSVFFPVFVR FIRSYKEAEQ ENEARKKQEE VMREKQLAQE AKKLDAKTPS
QRNKWQQQEL IAELRRRQAK EHRPVYEGKD GTIEDIITVL KSVPFTARTA KRGSRFFCDA
AHHDESNC
