SH3B4_HUMAN
ID SH3B4_HUMAN Reviewed; 963 AA.
AC Q9P0V3; O95082; Q309A3; Q53QD0; Q53TD1;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=SH3 domain-binding protein 4;
DE AltName: Full=EH-binding protein 10;
DE AltName: Full=Transferrin receptor-trafficking protein;
GN Name=SH3BP4; Synonyms=BOG25, EHB10, TTP;
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 1), AND TISSUE SPECIFICITY.
RC TISSUE=Corneal fibroblast;
RX PubMed=10644451; DOI=10.1006/geno.1999.5994;
RA Dunlevy J.R., Berryhill B.L., Vergnes J.-P., SundarRaj N., Hassell J.R.;
RT "Cloning, chromosomal localization, and characterization of cDNA from a
RT novel gene, SH3BP4, expressed by human corneal fibroblasts.";
RL Genomics 62:519-524(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION IN ENDOCYTOSIS,
RP INTERACTION WITH AP-2; CLATHRIN; DNM2; EPS15 AND TFRC, OLIGOMERIZATION,
RP PHOSPHORYLATION, SUBCELLULAR LOCATION, MUTAGENESIS OF TRP-92, AND VARIANTS
RP THR-155 AND THR-197.
RC TISSUE=Placenta;
RX PubMed=16325581; DOI=10.1016/j.cell.2005.10.021;
RA Tosoni D., Puri C., Confalonieri S., Salcini A.E., De Camilli P.,
RA Tacchetti C., Di Fiore P.P.;
RT "TTP specifically regulates the internalization of the transferrin
RT receptor.";
RL Cell 123:875-888(2005).
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 1).
RC TISSUE=Eye;
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 [MRNA] OF 74-963 (ISOFORM 2), AND INTERACTION WITH
RP EPS15.
RC TISSUE=Fibroblast;
RX PubMed=9303539; DOI=10.1101/gad.11.17.2239;
RA Salcini A.E., Confalonieri S., Doria M., Santolini E., Tassi E.,
RA Minenkova O., Cesareni G., Pelicci P.G., Di Fiore P.P.;
RT "Binding specificity and in vivo targets of the EH domain, a novel protein-
RT protein interaction module.";
RL Genes Dev. 11:2239-2249(1997).
RN [6]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15616480;
RA Khanobdee K., Kolberg J.B., Dunlevy J.R.;
RT "Nuclear and plasma membrane localization of SH3BP4 in retinal pigment
RT epithelial cells.";
RL Mol. Vis. 10:933-942(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246, 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-637, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP FUNCTION IN MTORC1 SIGNALING, INTERACTION WITH RRAGA; RRAGB; RRAGC AND
RP RRAGD, AND MUTAGENESIS OF TRP-92.
RX PubMed=22575674; DOI=10.1016/j.molcel.2012.04.007;
RA Kim Y.M., Stone M., Hwang T.H., Kim Y.G., Dunlevy J.R., Griffin T.J.,
RA Kim D.H.;
RT "SH3BP4 is a negative regulator of amino acid-Rag GTPase-mTORC1
RT signaling.";
RL Mol. Cell 46:833-846(2012).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246; SER-279 AND SER-637, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296, 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).
RN [14]
RP INTERACTION WITH MOLLUSCUM CONTAGIOSUM VIRUS PROTEIN MC159L (MICROBIAL
RP INFECTION).
RX PubMed=30842330; DOI=10.1128/jvi.01613-18;
RA Schmotz C., Ugurlu H., Vilen S., Shrestha S., Fagerlund R., Saksela K.;
RT "MC159 of molluscum contagiosum virus suppresses autophagy by recruiting
RT cellular SH3BP4 via an SH3 domain-mediated interaction.";
RL J. Virol. 0:0-0(2019).
CC -!- FUNCTION: May function in transferrin receptor internalization at the
CC plasma membrane through a cargo-specific control of clathrin-mediated
CC endocytosis. Alternatively, may act as a negative regulator of the
CC amino acid-induced TOR signaling by inhibiting the formation of active
CC Rag GTPase complexes. Preferentially binds inactive Rag GTPase
CC complexes and prevents their interaction with the mTORC1 complex
CC inhibiting its relocalization to lysosomes and its activation. Thereby,
CC may indirectly regulate cell growth, proliferation and autophagy.
CC {ECO:0000269|PubMed:16325581, ECO:0000269|PubMed:22575674}.
CC -!- SUBUNIT: Homodimer or homooligomer. Interacts with DNM2, EPS15,
CC clathrin, the adapter protein complex 2/AP-2 and TFRC. Interacts with
CC the Rag GTPases RRAGA, RRAGB, RRAGC and RRAGD; the interaction is most
CC probably direct, preferentially occurs with their inactive GDP-bound
CC form and is negatively regulated by amino acids.
CC {ECO:0000269|PubMed:16325581, ECO:0000269|PubMed:22575674,
CC ECO:0000269|PubMed:9303539}.
CC -!- SUBUNIT: (Microbial infection) Interacts with molluscum contagiosum
CC virus protein MC159L; this interaction is important for the suppression
CC of autophagy. {ECO:0000269|PubMed:30842330}.
CC -!- INTERACTION:
CC Q9P0V3; Q9ULV3: CIZ1; NbExp=2; IntAct=EBI-1049513, EBI-2652948;
CC Q9P0V3; P50570: DNM2; NbExp=3; IntAct=EBI-1049513, EBI-346547;
CC Q9P0V3; P42566: EPS15; NbExp=2; IntAct=EBI-1049513, EBI-396684;
CC Q9P0V3; Q9HB21: PLEKHA1; NbExp=2; IntAct=EBI-1049513, EBI-2652984;
CC Q9P0V3; Q9P0V3: SH3BP4; NbExp=2; IntAct=EBI-1049513, EBI-1049513;
CC Q9P0V3; P02786: TFRC; NbExp=6; IntAct=EBI-1049513, EBI-355727;
CC Q9P0V3; P39052: Dnm2; Xeno; NbExp=5; IntAct=EBI-1049513, EBI-349613;
CC -!- SUBCELLULAR LOCATION: Membrane, clathrin-coated pit. Cytoplasmic
CC vesicle, clathrin-coated vesicle. Nucleus {ECO:0000305}.
CC Note=Specifically associated with transferrin receptor-containing
CC clathrin-coated pits and clathrin-coated vesicles. May also localize to
CC the nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9P0V3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9P0V3-2; Sequence=VSP_022823;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues tested with higher
CC expression in pancreas. Expressed by retinal pigment epithelial cells
CC (at protein level). {ECO:0000269|PubMed:10644451,
CC ECO:0000269|PubMed:15616480}.
CC -!- DOMAIN: The SH3 domain mediates localization to the clathrin-coated
CC pits and vesicles. The SH3 domain mediates interaction with DNM2 and
CC the cytoplasmic part of TFRC with a lower affinity. The SH3 domain also
CC mediates interaction with RRAGB, RRAGC and is required for the negative
CC regulation of mTORC1.
CC -!- PTM: Phosphorylated upon EGF stimulation. Phosphorylation prevents
CC interaction with DNM2. {ECO:0000269|PubMed:16325581}.
CC -!- MISCELLANEOUS: Overexpression or depletion of SH3BP4 result in a
CC specific decrease of the transferrin receptor endocytosis that can be
CC rescued by DNM2 overexpression.
CC -!- MISCELLANEOUS: [Isoform 2]: Dubious isoform produced through aberrant
CC splice sites. {ECO:0000305}.
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DR EMBL; AF147747; AAF33022.1; -; mRNA.
DR EMBL; DQ232895; ABB18377.1; -; mRNA.
DR EMBL; AC010148; AAY14916.1; -; Genomic_DNA.
DR EMBL; AC114814; AAY24025.1; -; Genomic_DNA.
DR EMBL; BC057396; AAH57396.1; -; mRNA.
DR EMBL; AF015043; AAD01551.1; -; mRNA.
DR CCDS; CCDS2513.1; -. [Q9P0V3-1]
DR RefSeq; NP_055336.1; NM_014521.2. [Q9P0V3-1]
DR RefSeq; XP_011509193.1; XM_011510891.2.
DR RefSeq; XP_011509194.1; XM_011510892.1.
DR RefSeq; XP_011509195.1; XM_011510893.1. [Q9P0V3-1]
DR RefSeq; XP_011509196.1; XM_011510894.2.
DR AlphaFoldDB; Q9P0V3; -.
DR SMR; Q9P0V3; -.
DR BioGRID; 117194; 120.
DR IntAct; Q9P0V3; 49.
DR MINT; Q9P0V3; -.
DR STRING; 9606.ENSP00000386862; -.
DR iPTMnet; Q9P0V3; -.
DR PhosphoSitePlus; Q9P0V3; -.
DR BioMuta; SH3BP4; -.
DR DMDM; 74753102; -.
DR EPD; Q9P0V3; -.
DR jPOST; Q9P0V3; -.
DR MassIVE; Q9P0V3; -.
DR MaxQB; Q9P0V3; -.
DR PaxDb; Q9P0V3; -.
DR PeptideAtlas; Q9P0V3; -.
DR PRIDE; Q9P0V3; -.
DR ProteomicsDB; 83602; -. [Q9P0V3-1]
DR ProteomicsDB; 83603; -. [Q9P0V3-2]
DR Antibodypedia; 34462; 185 antibodies from 31 providers.
DR DNASU; 23677; -.
DR Ensembl; ENST00000344528.8; ENSP00000340237.4; ENSG00000130147.16. [Q9P0V3-1]
DR Ensembl; ENST00000392011.7; ENSP00000375867.2; ENSG00000130147.16. [Q9P0V3-1]
DR Ensembl; ENST00000409212.5; ENSP00000386862.1; ENSG00000130147.16. [Q9P0V3-1]
DR GeneID; 23677; -.
DR KEGG; hsa:23677; -.
DR MANE-Select; ENST00000392011.7; ENSP00000375867.2; NM_014521.3; NP_055336.1.
DR UCSC; uc002vvp.4; human. [Q9P0V3-1]
DR CTD; 23677; -.
DR DisGeNET; 23677; -.
DR GeneCards; SH3BP4; -.
DR HGNC; HGNC:10826; SH3BP4.
DR HPA; ENSG00000130147; Tissue enhanced (salivary).
DR MIM; 605611; gene.
DR neXtProt; NX_Q9P0V3; -.
DR OpenTargets; ENSG00000130147; -.
DR PharmGKB; PA35734; -.
DR VEuPathDB; HostDB:ENSG00000130147; -.
DR eggNOG; ENOG502QTUW; Eukaryota.
DR GeneTree; ENSGT00390000013151; -.
DR HOGENOM; CLU_013080_2_0_1; -.
DR InParanoid; Q9P0V3; -.
DR OMA; HRIRANN; -.
DR OrthoDB; 140316at2759; -.
DR PhylomeDB; Q9P0V3; -.
DR TreeFam; TF105572; -.
DR PathwayCommons; Q9P0V3; -.
DR Reactome; R-HSA-9639288; Amino acids regulate mTORC1.
DR SignaLink; Q9P0V3; -.
DR SIGNOR; Q9P0V3; -.
DR BioGRID-ORCS; 23677; 4 hits in 1070 CRISPR screens.
DR ChiTaRS; SH3BP4; human.
DR GeneWiki; SH3BP4; -.
DR GenomeRNAi; 23677; -.
DR Pharos; Q9P0V3; Tbio.
DR PRO; PR:Q9P0V3; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9P0V3; protein.
DR Bgee; ENSG00000130147; Expressed in parotid gland and 195 other tissues.
DR ExpressionAtlas; Q9P0V3; baseline and differential.
DR Genevisible; Q9P0V3; HS.
DR GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell.
DR GO; GO:0030136; C:clathrin-coated vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005092; F:GDP-dissociation inhibitor activity; IMP:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; IMP:UniProtKB.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0030308; P:negative regulation of cell growth; IMP:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0034260; P:negative regulation of GTPase activity; IDA:UniProtKB.
DR GO; GO:0032007; P:negative regulation of TOR signaling; IMP:UniProtKB.
DR GO; GO:0010508; P:positive regulation of autophagy; IMP:UniProtKB.
DR GO; GO:0061462; P:protein localization to lysosome; IMP:UniProtKB.
DR GO; GO:0050790; P:regulation of catalytic activity; IMP:UniProtKB.
DR CDD; cd11757; SH3_SH3BP4; 1.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR035455; SH3BP4.
DR InterPro; IPR035456; SH3BP4_SH3.
DR InterPro; IPR000906; ZU5_dom.
DR PANTHER; PTHR15603:SF3; PTHR15603:SF3; 1.
DR Pfam; PF00018; SH3_1; 1.
DR Pfam; PF07653; SH3_2; 1.
DR Pfam; PF00791; ZU5; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50002; SH3; 2.
DR PROSITE; PS51145; ZU5; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coated pit; Cytoplasmic vesicle; Endocytosis;
KW Membrane; Nucleus; Phosphoprotein; Reference proteome; Repeat; SH3 domain.
FT CHAIN 1..963
FT /note="SH3 domain-binding protein 4"
FT /id="PRO_0000274574"
FT DOMAIN 55..114
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 317..454
FT /note="ZU5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00485"
FT DOMAIN 654..724
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT MOD_RES 131
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT MOD_RES 246
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 251
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q921I6"
FT MOD_RES 279
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 296
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 637
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 515..925
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9303539"
FT /id="VSP_022823"
FT VARIANT 155
FT /note="M -> T (in dbSNP:rs3731644)"
FT /evidence="ECO:0000269|PubMed:16325581"
FT /id="VAR_030330"
FT VARIANT 197
FT /note="A -> T (in dbSNP:rs3731646)"
FT /evidence="ECO:0000269|PubMed:16325581"
FT /id="VAR_030331"
FT MUTAGEN 92
FT /note="W->A: Loss of function. Loss of targeting to the
FT clathrin-coated pits and vesicles. Loss of interaction with
FT DNM2, RRAGB and RRAGC. No effect on localization to the
FT plasma membrane."
FT /evidence="ECO:0000269|PubMed:16325581,
FT ECO:0000269|PubMed:22575674"
FT CONFLICT 235
FT /note="D -> N (in Ref. 2; ABB18377)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 963 AA; 107496 MW; 7F98200AC420F3D5 CRC64;
MAAQRIRAAN SNGLPRCKSE GTLIDLSEGF SETSFNDIKV PSPSALLVDN PTPFGNAKEV
IAIKDYCPTN FTTLKFSKGD HLYVLDTSGG EWWYAHNTTE MGYIPSSYVQ PLNYRNSTLS
DSGMIDNLPD SPDEVAKELE LLGGWTDDKK VPGRMYSNNP FWNGVQTNPF LNGNVPVMPS
LDELNPKSTV DLLLFDAGTS SFTESSSATT NSTGNIFDEL PVTNGLHAEP PVRRDNPFFR
SKRSYSLSEL SVLQAKSDAP TSSSFFTGLK SPAPEQFQSR EDFRTAWLNH RKLARSCHDL
DLLGQSPGWG QTQAVETNIV CKLDSSGGAV QLPDTSISIH VPEGHVAPGE TQQISMKALL
DPPLELNSDR SCSISPVLEV KLSNLEVKTS IILEMKVSAE IKNDLFSKST VGLQCLRSDS
KEGPYVSVPL NCSCGDTVQA QLHNLEPCMY VAVVAHGPSI LYPSTVWDFI NKKVTVGLYG
PKHIHPSFKT VVTIFGHDCA PKTLLVSEVT RQAPNPAPVA LQLWGKHQFV LSRPQDLKVC
MFSNMTNYEV KASEQAKVVR GFQLKLGKVS RLIFPITSQN PNELSDFTLR VQVKDDQEAI
LTQFCVQTPQ PPPKSAIKPS GQRRFLKKNE VGKIILSPFA TTTKYPTFQD RPVSSLKFGK
LLKTVVRQNK NHYLLEYKKG DGIALLSEER VRLRGQLWTK EWYIGYYQGR VGLVHTKNVL
VVGRARPSLC SGPELSTSVL LEQILRPCKF LTYIYASVRT LLMENISSWR SFADALGYVN
LPLTFFCRAE LDSEPERVAS VLEKLKEDCN NTENKERKSF QKELVMALLK MDCQGLVVRL
IQDFVLLTTA VEVAQRWREL AEKLAKVSKQ QMDAYESPHR DRNGVVDSEA MWKPAYDFLL
TWSHQIGDSY RDVIQELHLG LDKMKNPITK RWKHLTGTLI LVNSLDVLRA AAFSPADQDD
FVI
