FGD4_HUMAN
ID FGD4_HUMAN Reviewed; 766 AA.
AC Q96M96; Q6ULS2; Q8TCP6;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=FYVE, RhoGEF and PH domain-containing protein 4;
DE AltName: Full=Actin filament-binding protein frabin;
DE AltName: Full=FGD1-related F-actin-binding protein;
DE AltName: Full=Zinc finger FYVE domain-containing protein 6;
GN Name=FGD4; Synonyms=FRABP, ZFYVE6;
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 2).
RC TISSUE=Testis;
RA Lu L., Huang X.Y., Xu M., Yin L.L., Li J.M., Zhou Z.M., Sha J.H.;
RT "Cloning a new transcript of actin-filament binding protein frabin in
RT testis.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 MRNA] (ISOFORM 3).
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 [4]
RP FUNCTION.
RX PubMed=15133042; DOI=10.1074/jbc.m401592200;
RA Chen X.M., Splinter P.L., Tietz P.S., Huang B.Q., Billadeau D.D.,
RA LaRusso N.F.;
RT "Phosphatidylinositol 3-kinase and frabin mediate Cryptosporidium parvum
RT cellular invasion via activation of Cdc42.";
RL J. Biol. Chem. 279:31671-31678(2004).
RN [5]
RP INVOLVEMENT IN CMT4H, VARIANTS CMT4H ARG-298 AND THR-298, TISSUE
RP SPECIFICITY, AND ALTERNATIVE SPLICING.
RX PubMed=17564959; DOI=10.1086/518428;
RA Delague V., Jacquier A., Hamadouche T., Poitelon Y., Baudot C.,
RA Boccaccio I., Chouery E., Chaouch M., Kassouri N., Jabbour R., Grid D.,
RA Megarbane A., Haase G., Levy N.;
RT "Mutations in FGD4 encoding the Rho GDP/GTP exchange factor FRABIN cause
RT autosomal recessive Charcot-Marie-Tooth type 4H.";
RL Am. J. Hum. Genet. 81:1-16(2007).
RN [6]
RP INVOLVEMENT IN CMT4H, AND VARIANT CMT4H ARG-298.
RX PubMed=17564972; DOI=10.1086/518770;
RA Stendel C., Roos A., Deconinck T., Pereira J., Castagner F., Niemann A.,
RA Kirschner J., Korinthenberg R., Ketelsen U.-P., Battaloglu E., Parman Y.,
RA Nicholson G., Ouvrier R., Seeger J., De Jonghe P., Weis J., Kruettgen A.,
RA Rudnik-Schoeneborn S., Bergmann C., Suter U., Zerres K., Timmerman V.,
RA Relvas J.B., Senderek J.;
RT "Peripheral nerve demyelination caused by a mutant Rho GTPase guanine
RT nucleotide exchange factor, frabin/FGD4.";
RL Am. J. Hum. Genet. 81:158-164(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-702, AND IDENTIFICATION BY
RP 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).
CC -!- FUNCTION: Activates CDC42, a member of the Ras-like family of Rho- and
CC Rac proteins, by exchanging bound GDP for free GTP. Plays a role in
CC regulating the actin cytoskeleton and cell shape. Activates MAPK8 (By
CC similarity). {ECO:0000250, ECO:0000269|PubMed:15133042}.
CC -!- SUBUNIT: Homooligomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cell
CC projection, filopodium {ECO:0000250}. Note=Concentrated in filopodia
CC and poorly detected at lamellipodia. Binds along the sides of actin
CC fibers (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=Q96M96-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96M96-2; Sequence=VSP_013078, VSP_013082;
CC Name=3;
CC IsoId=Q96M96-3; Sequence=VSP_013079, VSP_013080, VSP_013081;
CC -!- TISSUE SPECIFICITY: Expressed in different tissues, including brain,
CC cerebellum, peripheral nerve, skeletal muscle, heart, uterus, placenta
CC and testis. {ECO:0000269|PubMed:17564959}.
CC -!- DOMAIN: The part of the protein spanning the actin filament-binding
CC domain together with the DH domain and the first PH domain is necessary
CC and sufficient for microspike formation. Activation of MAPK8 requires
CC the presence of all domains with the exception of the actin filament-
CC binding domain (By similarity). {ECO:0000250}.
CC -!- DISEASE: Charcot-Marie-Tooth disease 4H (CMT4H) [MIM:609311]: A
CC recessive demyelinating form of Charcot-Marie-Tooth disease, a disorder
CC of the peripheral nervous system, characterized by progressive weakness
CC and atrophy, initially of the peroneal muscles and later of the distal
CC muscles of the arms. Charcot-Marie-Tooth disease is classified in two
CC main groups on the basis of electrophysiologic properties and
CC histopathology: primary peripheral demyelinating neuropathies
CC (designated CMT1 when they are dominantly inherited) and primary
CC peripheral axonal neuropathies (CMT2). Demyelinating neuropathies are
CC characterized by severely reduced nerve conduction velocities (less
CC than 38 m/sec), segmental demyelination and remyelination with onion
CC bulb formations on nerve biopsy, slowly progressive distal muscle
CC atrophy and weakness, absent deep tendon reflexes, and hollow feet. By
CC convention autosomal recessive forms of demyelinating Charcot-Marie-
CC Tooth disease are designated CMT4. {ECO:0000269|PubMed:17564959,
CC ECO:0000269|PubMed:17564972}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
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DR EMBL; AY367054; AAQ72372.1; -; mRNA.
DR EMBL; AK057294; BAB71413.1; -; mRNA.
DR EMBL; AL713762; CAD28532.1; -; mRNA.
DR CCDS; CCDS8727.1; -. [Q96M96-1]
DR RefSeq; NP_001291409.1; NM_001304480.1.
DR RefSeq; NP_001317302.1; NM_001330373.1.
DR RefSeq; NP_001317303.1; NM_001330374.1.
DR RefSeq; NP_640334.2; NM_139241.3. [Q96M96-1]
DR RefSeq; XP_011518857.1; XM_011520555.1. [Q96M96-1]
DR RefSeq; XP_011518858.1; XM_011520556.1. [Q96M96-1]
DR AlphaFoldDB; Q96M96; -.
DR SMR; Q96M96; -.
DR BioGRID; 125734; 20.
DR IntAct; Q96M96; 6.
DR STRING; 9606.ENSP00000394487; -.
DR iPTMnet; Q96M96; -.
DR PhosphoSitePlus; Q96M96; -.
DR BioMuta; FGD4; -.
DR DMDM; 116241363; -.
DR EPD; Q96M96; -.
DR jPOST; Q96M96; -.
DR MassIVE; Q96M96; -.
DR MaxQB; Q96M96; -.
DR PaxDb; Q96M96; -.
DR PeptideAtlas; Q96M96; -.
DR PRIDE; Q96M96; -.
DR ProteomicsDB; 77320; -. [Q96M96-1]
DR ProteomicsDB; 77321; -. [Q96M96-2]
DR ProteomicsDB; 77322; -. [Q96M96-3]
DR Antibodypedia; 48934; 104 antibodies from 20 providers.
DR DNASU; 121512; -.
DR Ensembl; ENST00000427716.7; ENSP00000394487.2; ENSG00000139132.16. [Q96M96-1]
DR Ensembl; ENST00000525053.6; ENSP00000433666.2; ENSG00000139132.16. [Q96M96-1]
DR Ensembl; ENST00000583694.2; ENSP00000462623.2; ENSG00000139132.16. [Q96M96-1]
DR GeneID; 121512; -.
DR KEGG; hsa:121512; -.
DR UCSC; uc001rkz.5; human. [Q96M96-1]
DR CTD; 121512; -.
DR DisGeNET; 121512; -.
DR GeneCards; FGD4; -.
DR HGNC; HGNC:19125; FGD4.
DR HPA; ENSG00000139132; Low tissue specificity.
DR MalaCards; FGD4; -.
DR MIM; 609311; phenotype.
DR MIM; 611104; gene.
DR neXtProt; NX_Q96M96; -.
DR OpenTargets; ENSG00000139132; -.
DR Orphanet; 99954; Charcot-Marie-Tooth disease type 4H.
DR PharmGKB; PA134907925; -.
DR VEuPathDB; HostDB:ENSG00000139132; -.
DR eggNOG; KOG4424; Eukaryota.
DR GeneTree; ENSGT00940000155765; -.
DR InParanoid; Q96M96; -.
DR OMA; EREHSFY; -.
DR OrthoDB; 652460at2759; -.
DR PhylomeDB; Q96M96; -.
DR TreeFam; TF316247; -.
DR PathwayCommons; Q96M96; -.
DR Reactome; R-HSA-193648; NRAGE signals death through JNK.
DR Reactome; R-HSA-416482; G alpha (12/13) signalling events.
DR Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR SignaLink; Q96M96; -.
DR SIGNOR; Q96M96; -.
DR BioGRID-ORCS; 121512; 5 hits in 1063 CRISPR screens.
DR ChiTaRS; FGD4; human.
DR GeneWiki; FGD4; -.
DR GenomeRNAi; 121512; -.
DR Pharos; Q96M96; Tbio.
DR PRO; PR:Q96M96; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q96M96; protein.
DR Bgee; ENSG00000139132; Expressed in jejunal mucosa and 188 other tissues.
DR ExpressionAtlas; Q96M96; baseline and differential.
DR Genevisible; Q96M96; HS.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030175; C:filopodium; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:0001726; C:ruffle; ISS:UniProtKB.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031267; F:small GTPase binding; ISS:UniProtKB.
DR GO; GO:0030036; P:actin cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0007010; P:cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0046847; P:filopodium assembly; ISS:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB.
DR GO; GO:0043087; P:regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
DR CDD; cd15791; PH1_FDG4; 1.
DR CDD; cd13236; PH2_FGD1-4; 1.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 1.20.900.10; -; 1.
DR Gene3D; 2.30.29.30; -; 2.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR037742; FDG4_N_PH.
DR InterPro; IPR035941; FGD1-4_PH2.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF00169; PH; 2.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00064; FYVE; 1.
DR SMART; SM00233; PH; 2.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF48065; SSF48065; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 2.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Cell projection;
KW Charcot-Marie-Tooth disease; Cytoplasm; Cytoskeleton; Disease variant;
KW Guanine-nucleotide releasing factor; Metal-binding; Neurodegeneration;
KW Neuropathy; Phosphoprotein; Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..766
FT /note="FYVE, RhoGEF and PH domain-containing protein 4"
FT /id="PRO_0000080947"
FT DOMAIN 206..393
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 422..521
FT /note="PH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 643..740
FT /note="PH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT ZN_FING 559..619
FT /note="FYVE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT REGION 1..150
FT /note="Actin filament-binding"
FT /evidence="ECO:0000250"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 46..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 134..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 742..766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..188
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 752..766
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 565
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 568
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 582
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 585
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 590
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 593
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 611
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 614
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT MOD_RES 702
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 716
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91ZT5"
FT VAR_SEQ 1..248
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_013078"
FT VAR_SEQ 1..30
FT /note="MEEIKPASASCVSKEKPSKVSDLISRFEGG -> MFSCFLCILSF (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_013079"
FT VAR_SEQ 201..207
FT /note="ETNEQKL -> VEHETSS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_013080"
FT VAR_SEQ 208..766
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_013081"
FT VAR_SEQ 515..766
FT /note="ALQETIDAFHQRHETFRNAIAKDNDIHSEVSTAELGKRAPRWIRDNEVTMCM
FT KCKEPFNALTRRRHHCRACGYVVCWKCSDYKAQLEYDGGKLSKVCKDCYQIISGFTDSE
FT EKKRKGILEIESAEVSGNSVVCSFLQYMEKSKPWQKAWCVIPKQDPLVLYMYGAPQDVR
FT AQATIPLLGYVVDEMPRSADLPHSFKLTQSKSVHSFAADSEELKQKWLKVILLAVTGET
FT PGGPNEHPATLDDHPEPKKKSEC -> RRGFAMLPRLISNS (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_013082"
FT VARIANT 298
FT /note="M -> R (in CMT4H; found in patient's fibroblasts but
FT absent from peripheral nerve where splicing defects and
FT aberrant transcripts are detected; dbSNP:rs63749871)"
FT /evidence="ECO:0000269|PubMed:17564959,
FT ECO:0000269|PubMed:17564972"
FT /id="VAR_034957"
FT VARIANT 298
FT /note="M -> T (in CMT4H; dbSNP:rs63749871)"
FT /evidence="ECO:0000269|PubMed:17564959"
FT /id="VAR_044321"
FT CONFLICT 79
FT /note="T -> A (in Ref. 2; BAB71413)"
FT /evidence="ECO:0000305"
FT CONFLICT 303
FT /note="V -> A (in Ref. 1; AAQ72372)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 766 AA; 86626 MW; B919A7C1D164B05D CRC64;
MEEIKPASAS CVSKEKPSKV SDLISRFEGG SSLSNYSDLK KESAVNLNAP RTPGRHGLTT
TPQQKLLSQH LPQRQGNDTD KTQGAQTCVA NGVMAAQNQM ECEEEKAATL SSDTSIQASE
PLLDTHIVNG ERDETATAPA SPTTDSCDGN ASDSSYRTPG IGPVLPLEER GAETETKVQE
RENGESPLEL EQLDQHHEMK ETNEQKLHKI ANELLLTERA YVNRLDLLDQ VFYCKLLEEA
NRGSFPAEMV NKIFSNISSI NAFHSKFLLP ELEKRMQEWE TTPRIGDILQ KLAPFLKMYG
EYVKGFDNAM ELVKNMTERI PQFKSVVEEI QKQKICGSLT LQHHMLEPVQ RIPRYEMLLK
DYLRKLPPDS LDWNDAKKSL EIISTAASHS NSAIRKMENL KKLLEIYEML GEEEDIVNPS
NELIKEGQIL KLAARNTSAQ ERYLFLFNNM LLYCVPKFSL VGSKFTVRTR VGIDGMKIVE
TQNEEYPHTF QVSGKERTLE LQASSAQDKE EWIKALQETI DAFHQRHETF RNAIAKDNDI
HSEVSTAELG KRAPRWIRDN EVTMCMKCKE PFNALTRRRH HCRACGYVVC WKCSDYKAQL
EYDGGKLSKV CKDCYQIISG FTDSEEKKRK GILEIESAEV SGNSVVCSFL QYMEKSKPWQ
KAWCVIPKQD PLVLYMYGAP QDVRAQATIP LLGYVVDEMP RSADLPHSFK LTQSKSVHSF
AADSEELKQK WLKVILLAVT GETPGGPNEH PATLDDHPEP KKKSEC
