FCHO2_MOUSE
ID FCHO2_MOUSE Reviewed; 809 AA.
AC Q3UQN2; Q3UJ91; Q7TMS9; Q8C0I2;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=F-BAR domain only protein 2;
GN Name=Fcho2;
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 [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Amnion, Heart, and Thymus;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; 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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394; SER-402 AND SER-403, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-312; SER-387; SER-403;
RP SER-487; SER-492; SER-507; SER-509 AND SER-510, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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).
RN [5]
RP SUBCELLULAR LOCATION, INTERACTION WITH EPS15; EPS15R; ITSN1 AND ITSN2, AND
RP MUTAGENESIS OF PHE-38; TRP-73; LEU-136; LYS-146; LYS-165; ILE-268 AND
RP LYS-797.
RX PubMed=20448150; DOI=10.1126/science.1188462;
RA Henne W.M., Boucrot E., Meinecke M., Evergren E., Vallis Y., Mittal R.,
RA McMahon H.T.;
RT "FCHo proteins are nucleators of clathrin-mediated endocytosis.";
RL Science 328:1281-1284(2010).
RN [6]
RP FUNCTION IN LIPID-BINDING, SUBCELLULAR LOCATION, HOMOOLIGOMERIZATION,
RP INTERACTION WITH EPS15, UBIQUITINATION, AND TISSUE SPECIFICITY.
RX PubMed=21762413; DOI=10.1111/j.1365-2443.2011.01536.x;
RA Uezu A., Umeda K., Tsujita K., Suetsugu S., Takenawa T., Nakanishi H.;
RT "Characterization of the EFC/F-BAR domain protein, FCHO2.";
RL Genes Cells 16:868-878(2011).
RN [7]
RP FUNCTION IN CCV NUCLEATION.
RX PubMed=21883765; DOI=10.1111/j.1600-0854.2011.01273.x;
RA Nunez D., Antonescu C., Mettlen M., Liu A., Schmid S.L., Loerke D.,
RA Danuser G.;
RT "Hotspots organize clathrin-mediated endocytosis by efficient recruitment
RT and retention of nucleating resources.";
RL Traffic 12:1868-1878(2011).
RN [8]
RP INTERACTION WITH DAB2.
RX PubMed=22323290; DOI=10.1091/mbc.e11-09-0812;
RA Mulkearns E.E., Cooper J.A.;
RT "FCH domain only-2 organizes clathrin-coated structures and interacts with
RT Disabled-2 for low-density lipoprotein receptor endocytosis.";
RL Mol. Biol. Cell 23:1330-1342(2012).
CC -!- FUNCTION: Functions in an early step of clathrin-mediated endocytosis.
CC Has both a membrane binding/bending activity and the ability to recruit
CC proteins essential to the formation of functional clathrin-coated pits.
CC Has a lipid-binding activity with a preference for membranes enriched
CC in phosphatidylserine and phosphoinositides (Pi(4,5) biphosphate) like
CC the plasma membrane. Its membrane-bending activity might be important
CC for the subsequent action of clathrin and adaptors in the formation of
CC clathrin-coated vesicles. Involved in adaptor protein complex AP-2-
CC dependent endocytosis of the transferrin receptor, it also functions in
CC the AP-2-independent endocytosis of the LDL receptor.
CC {ECO:0000269|PubMed:21762413, ECO:0000269|PubMed:21883765}.
CC -!- SUBUNIT: Homodimer; disulfide-linked (By similarity). May form
CC homotetramer. Interacts with AP2A1. Interacts with EPS15, EPS15R, ITSN1
CC and ITSN2; recruit those scaffolding proteins which in turn may
CC interact with the adaptor protein complex AP-2 at the plasma membrane.
CC Interacts with DAB2 (via DPF motifs); mediates LDL receptor/LDLR
CC endocytosis. {ECO:0000250, ECO:0000269|PubMed:20448150,
CC ECO:0000269|PubMed:21762413, ECO:0000269|PubMed:22323290}.
CC -!- INTERACTION:
CC Q3UQN2; Q3UQN2: Fcho2; NbExp=5; IntAct=EBI-6094986, EBI-6094986;
CC Q3UQN2; P42566: EPS15; Xeno; NbExp=3; IntAct=EBI-6094986, EBI-396684;
CC Q3UQN2; Q15811: ITSN1; Xeno; NbExp=3; IntAct=EBI-6094986, EBI-602041;
CC Q3UQN2; A7BFV9; Xeno; NbExp=2; IntAct=EBI-6094986, EBI-6095043;
CC -!- SUBCELLULAR LOCATION: Membrane, clathrin-coated pit
CC {ECO:0000305|PubMed:20448150, ECO:0000305|PubMed:21762413}; Peripheral
CC membrane protein {ECO:0000305|PubMed:20448150,
CC ECO:0000305|PubMed:21762413}; Cytoplasmic side
CC {ECO:0000305|PubMed:20448150, ECO:0000305|PubMed:21762413}.
CC Note=Associated with forming but not mature clathrin-coated vesicles.
CC The recruitment to coated-pits precede the one of clathrin and the
CC adaptor protein complex AP-2.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q3UQN2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3UQN2-2; Sequence=VSP_021912, VSP_021913;
CC Name=3;
CC IsoId=Q3UQN2-3; Sequence=VSP_021914, VSP_021915;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed (at protein level).
CC {ECO:0000269|PubMed:21762413}.
CC -!- PTM: Ubiquitinated. Mainly undergoes monoubiquitination but also
CC polyubiquitination. {ECO:0000269|PubMed:21762413}.
CC -!- SIMILARITY: Belongs to the FCHO family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH52456.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH53718.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC27226.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC27226.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK031041; BAC27226.1; ALT_INIT; mRNA.
DR EMBL; AK142282; BAE25007.1; -; mRNA.
DR EMBL; AK146566; BAE27264.1; -; mRNA.
DR EMBL; BC052456; AAH52456.1; ALT_INIT; mRNA.
DR EMBL; BC053718; AAH53718.1; ALT_INIT; mRNA.
DR CCDS; CCDS56897.1; -. [Q3UQN2-1]
DR RefSeq; NP_766179.2; NM_172591.3. [Q3UQN2-1]
DR AlphaFoldDB; Q3UQN2; -.
DR SMR; Q3UQN2; -.
DR BioGRID; 230041; 51.
DR DIP; DIP-29489N; -.
DR IntAct; Q3UQN2; 18.
DR MINT; Q3UQN2; -.
DR STRING; 10090.ENSMUSP00000042959; -.
DR iPTMnet; Q3UQN2; -.
DR PhosphoSitePlus; Q3UQN2; -.
DR EPD; Q3UQN2; -.
DR jPOST; Q3UQN2; -.
DR MaxQB; Q3UQN2; -.
DR PaxDb; Q3UQN2; -.
DR PeptideAtlas; Q3UQN2; -.
DR PRIDE; Q3UQN2; -.
DR ProteomicsDB; 271734; -. [Q3UQN2-1]
DR ProteomicsDB; 271735; -. [Q3UQN2-2]
DR ProteomicsDB; 271736; -. [Q3UQN2-3]
DR Antibodypedia; 48744; 149 antibodies from 23 providers.
DR DNASU; 218503; -.
DR Ensembl; ENSMUST00000040340; ENSMUSP00000042959; ENSMUSG00000041685. [Q3UQN2-1]
DR Ensembl; ENSMUST00000109403; ENSMUSP00000105030; ENSMUSG00000041685. [Q3UQN2-2]
DR GeneID; 218503; -.
DR KEGG; mmu:218503; -.
DR UCSC; uc011zdl.2; mouse. [Q3UQN2-2]
DR UCSC; uc033gnc.1; mouse. [Q3UQN2-1]
DR CTD; 115548; -.
DR MGI; MGI:3505790; Fcho2.
DR VEuPathDB; HostDB:ENSMUSG00000041685; -.
DR eggNOG; KOG2398; Eukaryota.
DR GeneTree; ENSGT00940000157105; -.
DR HOGENOM; CLU_007107_0_0_1; -.
DR InParanoid; Q3UQN2; -.
DR OMA; IGMADTI; -.
DR OrthoDB; 638761at2759; -.
DR PhylomeDB; Q3UQN2; -.
DR TreeFam; TF328986; -.
DR Reactome; R-MMU-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
DR BioGRID-ORCS; 218503; 6 hits in 74 CRISPR screens.
DR ChiTaRS; Fcho2; mouse.
DR PRO; PR:Q3UQN2; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q3UQN2; protein.
DR Bgee; ENSMUSG00000041685; Expressed in dorsal pancreas and 226 other tissues.
DR ExpressionAtlas; Q3UQN2; baseline and differential.
DR Genevisible; Q3UQN2; MM.
DR GO; GO:0005905; C:clathrin-coated pit; IDA:UniProtKB.
DR GO; GO:0030136; C:clathrin-coated vesicle; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0098835; C:presynaptic endocytic zone membrane; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0035091; F:phosphatidylinositol binding; IDA:UniProtKB.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:UniProtKB.
DR GO; GO:0001786; F:phosphatidylserine binding; IDA:UniProtKB.
DR GO; GO:0048268; P:clathrin coat assembly; ISS:UniProtKB.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; ISS:UniProtKB.
DR GO; GO:0010324; P:membrane invagination; IDA:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; IMP:UniProtKB.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; IGI:ParkinsonsUK-UCL.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR030122; FCHo2.
DR InterPro; IPR028565; MHD.
DR InterPro; IPR018808; Muniscin_C.
DR PANTHER; PTHR23065:SF8; PTHR23065:SF8; 1.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF10291; muHD; 1.
DR SMART; SM00055; FCH; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS51072; MHD; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coated pit; Coiled coil; Disulfide bond; Endocytosis;
KW Isopeptide bond; Membrane; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..809
FT /note="F-BAR domain only protein 2"
FT /id="PRO_0000266006"
FT DOMAIN 3..250
FT /note="F-BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01077"
FT DOMAIN 541..808
FT /note="MHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00404"
FT REGION 3..274
FT /note="Mediates dimerization and binding to membranes
FT enriched in Pi(4,5)-P2 and induces their tubulation"
FT REGION 301..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 435..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 520..809
FT /note="Mediates interaction with DAB2, EPS15, EPS15R and
FT ITSN1"
FT /evidence="ECO:0000250"
FT COILED 87..156
FT /evidence="ECO:0000255"
FT COMPBIAS 390..420
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..454
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..536
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 312
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 385
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q0JRZ9"
FT MOD_RES 387
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 394
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 402
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 403
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 487
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 492
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 495
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q0JRZ9"
FT MOD_RES 507
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 509
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 510
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 532
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q0JRZ9"
FT DISULFID 147
FT /note="Interchain (with C-273)"
FT /evidence="ECO:0000250"
FT DISULFID 273
FT /note="Interchain (with C-147)"
FT /evidence="ECO:0000250"
FT CROSSLNK 297
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q0JRZ9"
FT VAR_SEQ 392..394
FT /note="RHS -> GFL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_021912"
FT VAR_SEQ 395..809
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_021913"
FT VAR_SEQ 404..414
FT /note="NEELTKSKPSS -> SKFDIGIGYFM (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_021914"
FT VAR_SEQ 415..809
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_021915"
FT MUTAGEN 38
FT /note="F->E: Loss of function mutant which is unable to
FT promote clathrin coated-pits formation. Cytosolic mutant;
FT when associated with E-73."
FT /evidence="ECO:0000269|PubMed:20448150"
FT MUTAGEN 73
FT /note="W->E: Loss of function mutant which is unable to
FT promote clathrin coated-pits formation. Cytosolic mutant;
FT when associated with E-38."
FT /evidence="ECO:0000269|PubMed:20448150"
FT MUTAGEN 136
FT /note="L->E: Loss of function mutant which is unable to
FT promote clathrin coated-pits formation. Binds to membrane
FT but is unable to induce membrane tubulation. Induces the
FT formation of large and static clathrin-coated pits."
FT /evidence="ECO:0000269|PubMed:20448150"
FT MUTAGEN 146
FT /note="K->E: Loss of function mutant which is unable to
FT promote clathrin coated-pits formation. Cytosolic mutant
FT which is unable to bind and induce membrane tubulation;
FT when associated with E-165."
FT /evidence="ECO:0000269|PubMed:20448150"
FT MUTAGEN 165
FT /note="K->E: Loss of function mutant which is unable to
FT promote clathrin coated-pits formation. Cytosolic mutant
FT which is unable to bind and induce membrane tubulation;
FT when associated with E-146."
FT /evidence="ECO:0000269|PubMed:20448150"
FT MUTAGEN 268
FT /note="I->N: Loss of function mutant which is unable to
FT promote clathrin coated-pits formation. Binds to membrane
FT but is unable to induce membrane tubulation. Induces the
FT formation of large and static clathrin-coated pits."
FT /evidence="ECO:0000269|PubMed:20448150"
FT MUTAGEN 797
FT /note="K->E: Loss of interaction with EPS15 and ITSN1."
FT /evidence="ECO:0000269|PubMed:20448150"
FT CONFLICT 13
FT /note="E -> K (in Ref. 1; BAC27226)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 809 AA; 88734 MW; 79FA8C2AFE6B606B CRC64;
MVMAHFVENF WGEKNNGFDV LYHNMKHGQI STKELADFVR ERATIEEAYS RSMTKLAKSA
SNYSQLGTFA PMWDVFKTST EKLANCHLDL VRKLQELIKE VQKYGEEQVK SHKKTKEEVA
GTLEAVQAIQ NITQALQKSK ENYTAKCVEQ ERLKKEGATQ REIEKAAVKS KKATDTYKLY
VEKYALTKAD FEQKMTETAQ KFQDIEETHL IHIKEIIGSL SNAVKEIHLQ IGQVHEEFIN
NMANTTIESL IQKFAESKGT GKERPGLIEF EECDPASAVE GIKPRKRKTF ALPGIIKKEK
DAESVECPDA DSLNIPDVDE EGFSIKPEAN QNDTKENHFY SSSDSDSEDE EPKRYRIEIK
PAHPNNLHHT MASLDELKVS IGNITLSPAV SRHSPVQMNR NSSNEELTKS KPSSLPTEKG
TNDLLAWDPL FGSSLESSSA PLTSSSSARP TTPLSLGTLV PPPRPASRPK LASGKLSGIN
EIPRPFSPPV TSNTSPPPTA PLARAESSSS ISSSASLSAA NTPTVGVSRG PSPVSLGNQD
TLPVAIALTE SVNAYFKGAD PTKCIVKITG DVTISFPSGI IKVFTSNPSP AVLCFRVKNI
SRLEQILPNS QLVFSDPSQC DSNTKDFWMN MQAVTIYLKK LSEQNPAASY YNVDVLKYQV
SSNGIQSTPL NLATYWKCSA STTDLRVDYK YNPEAMVAPS VLSNIQVVVP VDGGVTNMQS
LPPAIWNAEQ MKAFWKLSGI SEKSDSGGSG SLRAKFDLSE GPSKPTTLAV QFLSEGNTLS
GVDIELVGTG YRLSLVKKRF ATGRYLADC
