FCSD2_MOUSE
ID FCSD2_MOUSE Reviewed; 740 AA.
AC Q3USJ8; Q3UQZ2; Q6P9R0; Q80TS2;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=F-BAR and double SH3 domains protein 2;
DE AltName: Full=Protein nervous wreck 1 {ECO:0000303|PubMed:23761074, ECO:0000303|PubMed:26567222};
DE Short=NWK1 {ECO:0000303|PubMed:23761074, ECO:0000303|PubMed:26567222};
DE AltName: Full=SH3 multiple domains protein 3;
GN Name=Fchsd2; Synonyms=Kiaa0769, Sh3md3;
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] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Adipose tissue, and Spinal ganglion;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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 [4]
RP IDENTIFICATION.
RX PubMed=15067381;
RA Katoh M., Katoh M.;
RT "Identification and characterization of human FCHSD1 and FCHSD2 genes in
RT silico.";
RL Int. J. Mol. Med. 13:749-754(2004).
RN [5]
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, 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).
RN [7]
RP DOMAIN.
RX PubMed=23761074; DOI=10.1091/mbc.e13-05-0271;
RA Becalska A.N., Kelley C.F., Berciu C., Stanishneva-Konovalova T.B., Fu X.,
RA Wang S., Sokolova O.S., Nicastro D., Rodal A.A.;
RT "Formation of membrane ridges and scallops by the F-BAR protein Nervous
RT Wreck.";
RL Mol. Biol. Cell 24:2406-2418(2013).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, INTERACTION WITH WAS AND WASL, AND
RP TISSUE SPECIFICITY.
RX PubMed=23437151; DOI=10.1371/journal.pone.0056516;
RA Cao H., Yin X., Cao Y., Jin Y., Wang S., Kong Y., Chen Y., Gao J.,
RA Heller S., Xu Z.;
RT "FCHSD1 and FCHSD2 are expressed in hair cell stereocilia and cuticular
RT plate and regulate actin polymerization in vitro.";
RL PLoS ONE 8:E56516-E56516(2013).
RN [9]
RP DOMAIN.
RX PubMed=26686642; DOI=10.1016/j.celrep.2015.11.044;
RA Kelley C.F., Messelaar E.M., Eskin T.L., Wang S., Song K., Vishnia K.,
RA Becalska A.N., Shupliakov O., Hagan M.F., Danino D., Sokolova O.S.,
RA Nicastro D., Rodal A.A.;
RT "Membrane Charge Directs the Outcome of F-BAR Domain Lipid Binding and
RT Autoregulation.";
RL Cell Rep. 13:2597-2609(2015).
RN [10]
RP DEVELOPMENTAL STAGE.
RX PubMed=26567222; DOI=10.1242/jcs.178699;
RA Ukken F.P., Bruckner J.J., Weir K.L., Hope S.J., Sison S.L.,
RA Birschbach R.M., Hicks L., Taylor K.L., Dent E.W., Gonsalvez G.B.,
RA O'Connor-Giles K.M.;
RT "BAR-SH3 sorting nexins are conserved interacting proteins of Nervous wreck
RT that organize synapses and promote neurotransmission.";
RL J. Cell Sci. 129:166-177(2016).
RN [11]
RP INTERACTION WITH WASL.
RX PubMed=29887380; DOI=10.1016/j.cell.2018.05.020;
RA Almeida-Souza L., Frank R.A.W., Garcia-Nafria J., Colussi A.,
RA Gunawardana N., Johnson C.M., Yu M., Howard G., Andrews B., Vallis Y.,
RA McMahon H.T.;
RT "A Flat BAR Protein Promotes Actin Polymerization at the Base of Clathrin-
RT Coated Pits.";
RL Cell 174:325-337(2018).
CC -!- FUNCTION: Adapter protein that plays a role in endocytosis via
CC clathrin-coated pits. Contributes to the internalization of cell
CC surface receptors, such as integrin ITGB1 and transferrin receptor.
CC Promotes endocytosis of EGFR in cancer cells, and thereby contributes
CC to the down-regulation of EGFR signaling. Recruited to clathrin-coated
CC pits during a mid-to-late stage of assembly, where it is required for
CC normal progress from U-shaped intermediate stage pits to terminal,
CC omega-shaped pits. Binds to membranes enriched in phosphatidylinositol
CC 3,4-bisphosphate or phosphatidylinositol 3,4,5-trisphosphate (By
CC similarity). When bound to membranes, promotes actin polymerization via
CC its interaction with WAS and/or WASL which leads to the activation of
CC the Arp2/3 complex (PubMed:23437151). Does not promote actin
CC polymerisation in the absence of membranes (By similarity).
CC {ECO:0000250|UniProtKB:O94868, ECO:0000305|PubMed:23437151}.
CC -!- SUBUNIT: Homodimer (Probable). Interacts (via SH3 domain 2) with ITSN1
CC (via SH3 domain 4). Recruited to clathrin-coated pits during a mid-to-
CC late stage of assembly via interaction with ITSN1 (By similarity).
CC Interacts (via SH3 domain 1) with WASL (PubMed:23437151,
CC PubMed:29887380). Interacts with WAS (PubMed:23437151). Interacts with
CC CASK and MAGI1. CASK inhibits interaction with MAGI1 (By similarity).
CC {ECO:0000250|UniProtKB:O94868, ECO:0000269|PubMed:23437151,
CC ECO:0000269|PubMed:29887380, ECO:0000305|PubMed:23437151}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:23437151}. Cell
CC junction {ECO:0000250|UniProtKB:O94868}. Membrane, clathrin-coated pit
CC {ECO:0000250|UniProtKB:O94868}. Cell membrane
CC {ECO:0000250|UniProtKB:O94868}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:O94868}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:O94868}. Cell projection, stereocilium
CC {ECO:0000269|PubMed:23437151}. Note=Partially localized at clathrin-
CC coated pits at the cell membrane. Detected at the cell membrane at
CC sites around clathrin-coated pits, very close to the clathrin-coated
CC pits but not an intrinsic part of the clathrin-coated pits. Colocalizes
CC at cell-cell contacts with CDH1, but is not detected at tight
CC junctions. {ECO:0000250|UniProtKB:O94868}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q3USJ8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3USJ8-2; Sequence=VSP_023171;
CC Name=3;
CC IsoId=Q3USJ8-3; Sequence=VSP_023170, VSP_023171;
CC -!- TISSUE SPECIFICITY: Detected in inner ear vestibula and in stereocilia
CC in cochlear hair cell bundles (at protein level). Ubiquitous. Detected
CC in testis, liver, brain cortex, cerebellum, kidney, organ of Corti,
CC utricle, spiral ganglion, tongue and eye.
CC {ECO:0000269|PubMed:23437151}.
CC -!- DEVELOPMENTAL STAGE: Detected in brain cortex at 15.5 dpc and in
CC neonates, but levels decrease 16.5 days after birth and are very low in
CC adult brain cortex (at protein level). {ECO:0000269|PubMed:26567222}.
CC -!- DOMAIN: The F-BAR domain has an atypical, flat shape and binds
CC preferentially to flat membranes (By similarity). Upon heterologous
CC expression, the isolated F-BAR domain is localized at the cell
CC membrane, and causes the formation of cellular protrusions
CC (PubMed:23761074, PubMed:26686642). {ECO:0000250|UniProtKB:O94868,
CC ECO:0000269|PubMed:23761074, ECO:0000269|PubMed:26686642}.
CC -!- DOMAIN: Recruited to clathrin-coated pits via SH3 domain 2.
CC {ECO:0000250|UniProtKB:O94868}.
CC -!- DOMAIN: The two SH3 domains cooperate to maintain the protein in an
CC autoinhibited conformation that prevents promiscuous membrane binding.
CC {ECO:0000305|PubMed:26686642}.
CC -!- PTM: Phosphorylated. Phosphorylation on a Ser residue is important for
CC recruitment to the cell membrane and for its role in promoting
CC endocytosis. {ECO:0000250|UniProtKB:O94868}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC65650.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK122368; BAC65650.1; ALT_INIT; mRNA.
DR EMBL; AK140322; BAE24333.1; -; mRNA.
DR EMBL; AK141949; BAE24896.1; -; mRNA.
DR EMBL; BC060647; AAH60647.1; -; mRNA.
DR CCDS; CCDS52327.1; -. [Q3USJ8-2]
DR CCDS; CCDS52328.1; -. [Q3USJ8-1]
DR RefSeq; NP_001139482.1; NM_001146010.1. [Q3USJ8-1]
DR RefSeq; NP_950177.2; NM_199012.2. [Q3USJ8-2]
DR AlphaFoldDB; Q3USJ8; -.
DR SMR; Q3USJ8; -.
DR BioGRID; 228891; 2.
DR STRING; 10090.ENSMUSP00000032931; -.
DR iPTMnet; Q3USJ8; -.
DR PhosphoSitePlus; Q3USJ8; -.
DR EPD; Q3USJ8; -.
DR jPOST; Q3USJ8; -.
DR MaxQB; Q3USJ8; -.
DR PaxDb; Q3USJ8; -.
DR PeptideAtlas; Q3USJ8; -.
DR PRIDE; Q3USJ8; -.
DR ProteomicsDB; 270978; -. [Q3USJ8-1]
DR ProteomicsDB; 270979; -. [Q3USJ8-2]
DR ProteomicsDB; 270980; -. [Q3USJ8-3]
DR Antibodypedia; 49955; 105 antibodies from 20 providers.
DR DNASU; 207278; -.
DR Ensembl; ENSMUST00000032931; ENSMUSP00000032931; ENSMUSG00000030691. [Q3USJ8-2]
DR Ensembl; ENSMUST00000098250; ENSMUSP00000095850; ENSMUSG00000030691. [Q3USJ8-1]
DR GeneID; 207278; -.
DR KEGG; mmu:207278; -.
DR UCSC; uc009ioc.2; mouse. [Q3USJ8-2]
DR UCSC; uc009iod.2; mouse. [Q3USJ8-1]
DR CTD; 9873; -.
DR MGI; MGI:2448475; Fchsd2.
DR VEuPathDB; HostDB:ENSMUSG00000030691; -.
DR eggNOG; KOG3565; Eukaryota.
DR GeneTree; ENSGT00510000046732; -.
DR HOGENOM; CLU_013546_0_0_1; -.
DR InParanoid; Q3USJ8; -.
DR OMA; YADGWWE; -.
DR OrthoDB; 348563at2759; -.
DR PhylomeDB; Q3USJ8; -.
DR TreeFam; TF324557; -.
DR BioGRID-ORCS; 207278; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Fchsd2; mouse.
DR PRO; PR:Q3USJ8; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q3USJ8; protein.
DR Bgee; ENSMUSG00000030691; Expressed in animal zygote and 221 other tissues.
DR ExpressionAtlas; Q3USJ8; baseline and differential.
DR Genevisible; Q3USJ8; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005905; C:clathrin-coated pit; ISO:MGI.
DR GO; GO:0031594; C:neuromuscular junction; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0055037; C:recycling endosome; IBA:GO_Central.
DR GO; GO:0120043; C:stereocilium shaft; IDA:UniProtKB.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; ISS:UniProtKB.
DR GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; ISS:UniProtKB.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; ISS:UniProtKB.
DR GO; GO:0061024; P:membrane organization; IMP:GO_Central.
DR GO; GO:0007274; P:neuromuscular synaptic transmission; IBA:GO_Central.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IDA:UniProtKB.
DR GO; GO:2000601; P:positive regulation of Arp2/3 complex-mediated actin nucleation; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0030833; P:regulation of actin filament polymerization; IBA:GO_Central.
DR CDD; cd11894; SH3_FCHSD2_2; 1.
DR CDD; cd11761; SH3_FCHSD_1; 1.
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; IPR034934; FCHSD2.
DR InterPro; IPR035556; FCHSD2_SH3_2.
DR InterPro; IPR035460; FCHSD_SH3_1.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR15735:SF11; PTHR15735:SF11; 1.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF00018; SH3_1; 1.
DR Pfam; PF14604; SH3_9; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00055; FCH; 1.
DR SMART; SM00326; SH3; 2.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF50044; SSF50044; 2.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS50002; SH3; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell junction; Cell membrane; Cell projection;
KW Coated pit; Coiled coil; Cytoplasm; Endocytosis; Lipid-binding; Membrane;
KW Phosphoprotein; Protein transport; Reference proteome; Repeat; SH3 domain;
KW Transport.
FT CHAIN 1..740
FT /note="F-BAR and double SH3 domains protein 2"
FT /id="PRO_0000278215"
FT DOMAIN 8..282
FT /note="F-BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01077"
FT DOMAIN 469..530
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 567..629
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 303..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 567..629
FT /note="Required and sufficient for location at clathrin-
FT coated pits"
FT /evidence="ECO:0000250|UniProtKB:O94868"
FT REGION 629..740
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 356..397
FT /evidence="ECO:0000255"
FT COMPBIAS 631..647
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 648..669
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 670..707
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 675
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94868"
FT MOD_RES 681
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94868"
FT VAR_SEQ 1..38
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023170"
FT VAR_SEQ 308
FT /note="T -> TSLKAAQLVDIELSPVSALRMTIAE (in isoform 2 and
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:12693553,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_023171"
FT CONFLICT 350
FT /note="N -> D (in Ref. 2; BAE24333)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 740 AA; 84282 MW; 31BB6275D922AE8E CRC64;
MQPPPRKVKV TQELRNIQGE QMTKLQAKHQ AECDLLEDMR TFSQKKAAIE REYAQGIQKL
ASQYLKRDWP GIKTDDRNDY RSMYPVWKSF LEGTMQVAQS RINICENYKN FISEPARAVR
SLKEQQLKRC VDQLTKIQTE LQETVKDLVK GKKKYFETEQ MAHAVREKAD IEAKSKLSLF
QSRISLQKAS VKLKARRSEC NTKATHARND YLLTLAAANA HQDRYYQTDL VNIMKALDGN
VYDHLKDYLI AFSRTELETC QAIQNTFQFL LENSSKVVRD YNLQLFLQEN AVFHKPQPFQ
FQPCDSDTSR QLESETGTTE EHSLNKEARK WATRVAREHK NIVHQQRVLN ELECHGVALS
EQSRAELEQK IDEARESIRK AEIIKLKAEA RLDLLKQIGV SVDTWLKSAM NQVMEELENE
RWARPPAVTS NGTLHSLNAD AEREEGEEFE DNMDVFDDSS SSPSGTLRNY PLTCKVVYSY
KASQPDELTI EEHEVLEVIE DGDMEDWVKA RNKVGQVGYV PEKYLQFPTS NSLLSMLQSL
AALDSRSHTS SNSTEAELVS GSLNGDASVC FVKALYDYEG QTDDELSFPE GAIIRILNKE
NQDDDGFWEG EFSGRIGVFP SVLVEELSAS ENGDTPWTRE IQISPSPKPH TSLPPLPLYD
QPPSSPYPSP DKRSSQFFPR SPSANENSLH AESPGFSQAS RQTPDTSYGK LRPVRAAPPP
PTQNHRRTTE KMEDVEITLV
