ID   GGYF1_HUMAN             Reviewed;        1035 AA.
AC   O75420; Q6Y7W7; Q8WZ38;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 2.
DT   28-JAN-2026, entry version 174.
DE   RecName: Full=GRB10-interacting GYF protein 1;
DE   AltName: Full=PERQ amino acid-rich with GYF domain-containing protein 1;
GN   Name=GIGYF1; Synonyms=CDS2, PERQ1; ORFNames=PP3360;
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 [GENOMIC DNA].
RX   PubMed=9799793; DOI=10.1101/gr.8.10.1060;
RA   Gloeckner G., Scherer S., Schattevoy R., Boright A.P., Weber J.,
RA   Tsui L.-C., Rosenthal A.;
RT   "Large-scale sequencing of two regions in human chromosome 7q22: analysis
RT   of 650 kb of genomic sequence around the EPO and CUTL1 loci reveals 17
RT   genes.";
RL   Genome Res. 8:1060-1073(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   TISSUE=Placenta;
RX   PubMed=12771153; DOI=10.1074/jbc.m211572200;
RA   Giovannone B., Lee E., Laviola L., Giorgino F., Cleveland K.A., Smith R.J.;
RT   "Two novel proteins that are linked to insulin-like growth factor (IGF-I)
RT   receptors by the Grb10 adapter and modulate IGF-I signaling.";
RL   J. Biol. Chem. 278:31564-31573(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 729-1035.
RX   PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA   Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA   Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA   Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT   "Large-scale cDNA transfection screening for genes related to cancer
RT   development and progression.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-638, 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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24 AND SER-28, AND
RP   IDENTIFICATION BY 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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24; SER-137; SER-157;
RP   SER-406; SER-538; SER-638 AND SER-862, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, 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   [9]
RP   INTERACTION WITH DDX6, AND MUTAGENESIS OF TRP-294; PHE-306 AND PHE-312.
RX   PubMed=31439631; DOI=10.1101/gad.329219.119;
RA   Peter D., Ruscica V., Bawankar P., Weber R., Helms S., Valkov E.,
RA   Igreja C., Izaurralde E.;
RT   "Molecular basis for GIGYF-Me31B complex assembly in 4EHP-mediated
RT   translational repression.";
RL   Genes Dev. 33:1355-1360(2019).
CC   -!- FUNCTION: May act cooperatively with GRB10 to regulate tyrosine kinase
CC       receptor signaling. May increase IGF1 receptor phosphorylation under
CC       IGF1 stimulation as well as phosphorylation of IRS1 and SHC1 (By
CC       similarity). {ECO:0000250, ECO:0000269|PubMed:12771153}.
CC   -!- SUBUNIT: Interacts with GRB10 (By similarity). This transient binding
CC       is increased under IGF1 stimulation and leads to recruitment of
CC       GIGYF1/GRB10 complex to IGF1 receptor (By similarity). Interacts with
CC       DDX6 (PubMed:31439631). {ECO:0000250|UniProtKB:Q99MR1,
CC       ECO:0000269|PubMed:31439631}.
CC   -!- INTERACTION:
CC       O75420; Q9NX04: AIRIM; NbExp=3; IntAct=EBI-947774, EBI-8643161;
CC       O75420; Q9NXR5-2: ANKRD10; NbExp=3; IntAct=EBI-947774, EBI-12102070;
CC       O75420; Q9H6L4: ARMC7; NbExp=3; IntAct=EBI-947774, EBI-742909;
CC       O75420; Q9HC52: CBX8; NbExp=3; IntAct=EBI-947774, EBI-712912;
CC       O75420; Q2TAC2-2: CCDC57; NbExp=3; IntAct=EBI-947774, EBI-10961624;
CC       O75420; Q9BSW2: CRACR2A; NbExp=3; IntAct=EBI-947774, EBI-739773;
CC       O75420; P26196: DDX6; NbExp=5; IntAct=EBI-947774, EBI-351257;
CC       O75420; Q14204: DYNC1H1; NbExp=2; IntAct=EBI-947774, EBI-356015;
CC       O75420; O60573: EIF4E2; NbExp=5; IntAct=EBI-947774, EBI-398610;
CC       O75420; O60573-1: EIF4E2; NbExp=12; IntAct=EBI-947774, EBI-32715389;
CC       O75420; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-947774, EBI-744099;
CC       O75420; Q9H5Z6-2: FAM124B; NbExp=3; IntAct=EBI-947774, EBI-11986315;
CC       O75420; Q92993: KAT5; NbExp=3; IntAct=EBI-947774, EBI-399080;
CC       O75420; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-947774, EBI-14069005;
CC       O75420; Q96EZ8: MCRS1; NbExp=3; IntAct=EBI-947774, EBI-348259;
CC       O75420; Q8NEH6: MNS1; NbExp=3; IntAct=EBI-947774, EBI-743811;
CC       O75420; Q9HC98-4: NEK6; NbExp=3; IntAct=EBI-947774, EBI-11750983;
CC       O75420; Q8NI38: NFKBID; NbExp=3; IntAct=EBI-947774, EBI-10271199;
CC       O75420; P54646: PRKAA2; NbExp=3; IntAct=EBI-947774, EBI-1383852;
CC       O75420; P0CG20: PRR35; NbExp=3; IntAct=EBI-947774, EBI-11986293;
CC       O75420; Q9NW64: RBM22; NbExp=3; IntAct=EBI-947774, EBI-2602260;
CC       O75420; Q9UPN6: SCAF8; NbExp=3; IntAct=EBI-947774, EBI-7954236;
CC       O75420; Q9BWG6: SCNM1; NbExp=3; IntAct=EBI-947774, EBI-748391;
CC       O75420; Q8TAQ2: SMARCC2; NbExp=3; IntAct=EBI-947774, EBI-357418;
CC       O75420; Q96GM5: SMARCD1; NbExp=3; IntAct=EBI-947774, EBI-358489;
CC       O75420; P09012: SNRPA; NbExp=3; IntAct=EBI-947774, EBI-607085;
CC       O75420; P14678-2: SNRPB; NbExp=5; IntAct=EBI-947774, EBI-372475;
CC       O75420; P09234: SNRPC; NbExp=3; IntAct=EBI-947774, EBI-766589;
CC       O75420; Q99932-2: SPAG8; NbExp=3; IntAct=EBI-947774, EBI-11959123;
CC       O75420; Q96MF2: STAC3; NbExp=4; IntAct=EBI-947774, EBI-745680;
CC       O75420; Q15560: TCEA2; NbExp=3; IntAct=EBI-947774, EBI-710310;
CC       O75420; Q08117-2: TLE5; NbExp=3; IntAct=EBI-947774, EBI-11741437;
CC       O75420; Q12815: TROAP; NbExp=3; IntAct=EBI-947774, EBI-2349743;
CC       O75420; Q9NRE2: TSHZ2; NbExp=3; IntAct=EBI-947774, EBI-10687282;
CC       O75420; Q86UK7: ZNF598; NbExp=2; IntAct=EBI-947774, EBI-719433;
CC   -!- DOMAIN: The GYF domain interacts with GRB10. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the GIGYF family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC78792.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AAL55738.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AF053356; AAC78792.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AY176044; AAO46888.1; -; mRNA.
DR   EMBL; AF289554; AAL55738.1; ALT_FRAME; mRNA.
DR   CCDS; CCDS34708.1; -.
DR   RefSeq; NP_001362694.1; NM_001375765.1.
DR   RefSeq; NP_001362695.1; NM_001375766.1.
DR   PDB; 5NVK; X-ray; 2.90 A; B/D/F/H=33-103.
DR   PDB; 7RUQ; X-ray; 1.79 A; A/C=470-538.
DR   PDBsum; 5NVK; -.
DR   PDBsum; 7RUQ; -.
DR   AlphaFoldDB; O75420; -.
DR   SMR; O75420; -.
DR   BioGRID; 122218; 262.
DR   ComplexPortal; CPX-2336; 4EHP-GIGYF1 co-translational mRNA decay complex, ZNF598 variant.
DR   ComplexPortal; CPX-2342; 4EHP-GIGYF1 co-translational mRNA decay complex, DDX6 variant.
DR   FunCoup; O75420; 1093.
DR   IntAct; O75420; 178.
DR   MINT; O75420; -.
DR   STRING; 9606.ENSP00000275732; -.
DR   GlyCosmos; O75420; 1 site, 1 glycan.
DR   GlyGen; O75420; 2 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; O75420; -.
DR   PhosphoSitePlus; O75420; -.
DR   BioMuta; GIGYF1; -.
DR   jPOST; O75420; -.
DR   MassIVE; O75420; -.
DR   PaxDb; 9606-ENSP00000275732; -.
DR   PeptideAtlas; O75420; -.
DR   ProteomicsDB; 49992; -.
DR   Pumba; O75420; -.
DR   Antibodypedia; 16628; 82 antibodies from 16 providers.
DR   DNASU; 64599; -.
DR   Ensembl; ENST00000275732.5; ENSP00000275732.4; ENSG00000146830.12.
DR   Ensembl; ENST00000646601.1; ENSP00000494292.1; ENSG00000146830.12.
DR   Ensembl; ENST00000678049.1; ENSP00000503354.1; ENSG00000146830.12.
DR   GeneID; 64599; -.
DR   KEGG; hsa:64599; -.
DR   MANE-Select; ENST00000678049.1; ENSP00000503354.1; NM_001375765.1; NP_001362694.1.
DR   UCSC; uc003uwg.2; human.
DR   AGR; HGNC:9126; -.
DR   ClinPGx; PA162389554; -.
DR   CTD; 64599; -.
DR   GeneCards; GIGYF1; -.
DR   HGNC; HGNC:9126; GIGYF1.
DR   HPA; ENSG00000146830; Low tissue specificity.
DR   MalaCards; GIGYF1; -.
DR   MIM; 612064; gene.
DR   OpenTargets; ENSG00000146830; -.
DR   VEuPathDB; HostDB:ENSG00000146830; -.
DR   eggNOG; KOG1862; Eukaryota.
DR   GeneTree; ENSGT00940000159845; -.
DR   HOGENOM; CLU_007300_0_0_1; -.
DR   InParanoid; O75420; -.
DR   OMA; FHNTGEC; -.
DR   OrthoDB; 48509at2759; -.
DR   PAN-GO; O75420; 2 GO annotations based on evolutionary models.
DR   PhylomeDB; O75420; -.
DR   PathwayCommons; O75420; -.
DR   SignaLink; O75420; -.
DR   SIGNOR; O75420; -.
DR   Agora; ENSG00000146830; -.
DR   BioGRID-ORCS; 64599; 27 hits in 1151 CRISPR screens.
DR   CD-CODE; DEE660B4; Stress granule.
DR   ChiTaRS; GIGYF1; human.
DR   GenomeRNAi; 64599; -.
DR   Pharos; O75420; Tbio.
DR   PRO; PR:O75420; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   RNAct; O75420; protein.
DR   Bgee; ENSG00000146830; Expressed in sural nerve and 170 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR   GO; GO:0048009; P:insulin-like growth factor receptor signaling pathway; IBA:GO_Central.
DR   CDD; cd00072; GYF; 1.
DR   FunFam; 3.30.1490.40:FF:000001; GRB10-interacting GYF protein 2 isoform X1; 1.
DR   Gene3D; 3.30.1490.40; -; 1.
DR   InterPro; IPR051640; GRB10-interact_GYF.
DR   InterPro; IPR003169; GYF.
DR   InterPro; IPR035445; GYF-like_dom_sf.
DR   PANTHER; PTHR14445; GRB10 INTERACTING GYF PROTEIN; 1.
DR   PANTHER; PTHR14445:SF37; GRB10-INTERACTING GYF PROTEIN 1; 1.
DR   Pfam; PF02213; GYF; 1.
DR   SMART; SM00444; GYF; 1.
DR   SUPFAM; SSF55277; GYF domain; 1.
DR   PROSITE; PS50829; GYF; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Phosphoprotein; Proteomics identification;
KW   Reference proteome.
FT   CHAIN           1..1035
FT                   /note="GRB10-interacting GYF protein 1"
FT                   /id="PRO_0000058314"
FT   DOMAIN          474..522
FT                   /note="GYF"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00101"
FT   REGION          105..422
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          621..640
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          696..724
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          825..879
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        148..179
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        186..203
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        239..267
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        295..304
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        324..349
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        367..378
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        388..401
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        406..417
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        629..639
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        696..722
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        857..874
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         24
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         28
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231"
FT   MOD_RES         137
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19690332,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         157
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         230
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         341
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99MR1"
FT   MOD_RES         406
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         538
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         638
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         862
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MUTAGEN         294
FT                   /note="W->A: Abolishes interaction with DDX6."
FT                   /evidence="ECO:0000269|PubMed:31439631"
FT   MUTAGEN         306
FT                   /note="F->A: Abolishes interaction with DDX6; when
FT                   associated with A-312."
FT                   /evidence="ECO:0000269|PubMed:31439631"
FT   MUTAGEN         312
FT                   /note="F->A: Abolishes interaction with DDX6; when
FT                   associated with A-306."
FT                   /evidence="ECO:0000269|PubMed:31439631"
FT   CONFLICT        729..730
FT                   /note="RK -> DE (in Ref. 3; AAL55738)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        835
FT                   /note="S -> T (in Ref. 3; AAL55738)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        851
FT                   /note="L -> V (in Ref. 3; AAL55738)"
FT                   /evidence="ECO:0000305"
FT   HELIX           43..48
FT                   /evidence="ECO:0007829|PDB:5NVK"
FT   HELIX           58..61
FT                   /evidence="ECO:0007829|PDB:5NVK"
FT   HELIX           63..65
FT                   /evidence="ECO:0007829|PDB:5NVK"
FT   TURN            66..68
FT                   /evidence="ECO:0007829|PDB:5NVK"
FT   HELIX           77..79
FT                   /evidence="ECO:0007829|PDB:5NVK"
FT   HELIX           84..92
FT                   /evidence="ECO:0007829|PDB:5NVK"
FT   HELIX           97..100
FT                   /evidence="ECO:0007829|PDB:5NVK"
FT   STRAND          475..480
FT                   /evidence="ECO:0007829|PDB:7RUQ"
FT   STRAND          486..491
FT                   /evidence="ECO:0007829|PDB:7RUQ"
FT   HELIX           492..501
FT                   /evidence="ECO:0007829|PDB:7RUQ"
FT   STRAND          509..512
FT                   /evidence="ECO:0007829|PDB:7RUQ"
FT   STRAND          515..517
FT                   /evidence="ECO:0007829|PDB:7RUQ"
FT   HELIX           521..528
FT                   /evidence="ECO:0007829|PDB:7RUQ"
SQ   SEQUENCE   1035 AA;  114601 MW;  7DACB6F80EBEA7D0 CRC64;
     MAAETLNFGP EWLRALSGGG SVASPPPSPA MPKYKLADYR YGREEMLALY VKENKVPEEL
     QDKEFAAVLQ DEPLQPLALE PLTEEEQRNF SLSVNSVAVL RLMGKGAGPP LAGTSRGRGS
     TRSRGRGRGD SCFYQRSIEE GDGAFGRSPR EIQRSQSWDD RGERRFEKSA RRDGARCGFE
     EGGAGPRKEH ARSDSENWRS LREEQEEEEE GSWRLGAGPR RDGDRWRSAS PDGGPRSAGW
     REHGERRRKF EFDLRGDRGG CGEEEGRGGG GSSHLRRCRA PEGFEEDKDG LPEWCLDDED
     EEMGTFDASG AFLPLKKGPK EPIPEEQELD FQGLEEEEEP SEGLEEEGPE AGGKELTPLP
     PQEEKSSSPS PLPTLGPLWG TNGDGDETAE KEPPAAEDDI RGIQLSPGVG SSAGPPGDLE
     DDEGLKHLQQ EAEKLVASLQ DSSLEEEQFT AAMQTQGLRH SAAATALPLS HGAARKWFYK
     DPQGEIQGPF TTQEMAEWFQ AGYFSMSLLV KRGCDEGFQP LGEVIKMWGR VPFAPGPSPP
     PLLGNMDQER LKKQQELAAA ALYQQLQHQQ FLQLVSSRQL PQCALREKAA LGDLTPPPPP
     PPQQQQQQLT AFLQQLQALK PPRGGDQNLL PTMSRSLSVP DSGRLWDVHT SASSQSGGEA
     SLWDIPINSS TQGPILEQLQ LQHKFQERRE VELRAKREEE ERKRREEKRR QQQQEEQKRR
     QEEEELFRRK HVRQQELLLK LLQQQQAVPV PPAPSSPPPL WAGLAKQGLS MKTLLELQLE
     GERQLHKQPP PREPARAQAP NHRVQLGGLG TAPLNQWVSE AGPLWGGPDK SGGGSSGLGL
     WEDTPKSGGS LVRGLGLKNS RSSPSLSDSY SHLSGRPIRK KTEEEEKLLK LLQGIPRPQD
     GFTQWCEQML HTLSATGSLD VPMAVAILKE VESPYDVHDY IRSCLGDTLE AKEFAKQFLE
     RRAKQKASQQ RQQQQEAWLS SASLQTAFQA NHSTKLGPGE GSKAKRRALM LHSDPSILGY
     SLHGSSGEIE SVDDY
//