ID   FBX31_HUMAN             Reviewed;         539 AA.
AC   Q5XUX0; Q5K680; Q8WYV1; Q96D73; Q9UFV4;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 2.
DT   27-MAR-2024, entry version 159.
DE   RecName: Full=F-box only protein 31;
GN   Name=FBXO31; Synonyms=FBX14, FBX31; ORFNames=PP2386;
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).
RX   PubMed=15520277; DOI=10.1101/gad.1255304;
RA   Jin J., Cardozo T., Lovering R.C., Elledge S.J., Pagano M., Harper J.W.;
RT   "Systematic analysis and nomenclature of mammalian F-box proteins.";
RL   Genes Dev. 18:2573-2580(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Choriocarcinoma;
RA   Banham A.H., Cordell J.L., Jones M., Liggins A.P., Pulford K., Mason D.Y.;
RT   "A novel F-box protein is differentially expressed in hematopoietic
RT   malignancies.";
RL   Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15616553; DOI=10.1038/nature03187;
RA   Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA   Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA   Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA   Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA   Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA   Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA   Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA   Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA   Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA   Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA   Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA   Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA   Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA   Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA   Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA   Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA   Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA   Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA   Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA   DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA   Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA   Myers R.M., Rubin E.M., Pennacchio L.A.;
RT   "The sequence and analysis of duplication-rich human chromosome 16.";
RL   Nature 432:988-994(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Placenta;
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 149-539 (ISOFORM 1).
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   [7]
RP   TISSUE SPECIFICITY, SUBUNIT, FUNCTION, AND DEVELOPMENTAL STAGE.
RX   PubMed=16357137; DOI=10.1158/0008-5472.can-05-0936;
RA   Kumar R., Neilsen P.M., Crawford J., McKirdy R., Lee J., Powell J.A.,
RA   Saif Z., Martin J.M., Lombaerts M., Cornelisse C.J., Cleton-Jansen A.-M.,
RA   Callen D.F.;
RT   "FBXO31 is the chromosome 16q24.3 senescence gene, a candidate breast tumor
RT   suppressor, and a component of an SCF complex.";
RL   Cancer Res. 65:11304-11313(2005).
RN   [8]
RP   FUNCTION, IDENTIFICATION IN A SCF PROTEIN LIGASE COMPLEX, INDUCTION,
RP   INTERACTION WITH CCND1, PHOSPHORYLATION AT SER-278, AND MUTAGENESIS OF
RP   SER-278 AND SER-400.
RX   PubMed=19412162; DOI=10.1038/nature08011;
RA   Santra M.K., Wajapeyee N., Green M.R.;
RT   "F-box protein FBXO31 mediates cyclin D1 degradation to induce G1 arrest
RT   after DNA damage.";
RL   Nature 459:722-725(2009).
RN   [9]
RP   INVOLVEMENT IN MRT45.
RX   PubMed=24623383; DOI=10.1007/s00439-014-1438-0;
RA   Mir A., Sritharan K., Mittal K., Vasli N., Araujo C., Jamil T., Rafiq M.A.,
RA   Anwar Z., Mikhailov A., Rauf S., Mahmood H., Shakoor A., Ali S., So J.,
RA   Naeem F., Ayub M., Vincent J.B.;
RT   "Truncation of the E3 ubiquitin ligase component FBXO31 causes non-
RT   syndromic autosomal recessive intellectual disability in a Pakistani
RT   family.";
RL   Hum. Genet. 133:975-984(2014).
CC   -!- FUNCTION: Component of some SCF (SKP1-cullin-F-box) protein ligase
CC       complex that plays a central role in G1 arrest following DNA damage.
CC       Specifically recognizes phosphorylated cyclin-D1 (CCND1), promoting its
CC       ubiquitination and degradation by the proteasome, resulting in G1
CC       arrest. May act as a tumor suppressor. {ECO:0000269|PubMed:16357137,
CC       ECO:0000269|PubMed:19412162}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Part of a SCF (SKP1-cullin-F-box) protein ligase complex.
CC       {ECO:0000269|PubMed:16357137, ECO:0000269|PubMed:19412162}.
CC   -!- INTERACTION:
CC       Q5XUX0; Q13315: ATM; NbExp=2; IntAct=EBI-6162477, EBI-495465;
CC       Q5XUX0; P24385: CCND1; NbExp=4; IntAct=EBI-6162477, EBI-375001;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q5XUX0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5XUX0-2; Sequence=VSP_037469;
CC   -!- TISSUE SPECIFICITY: Highly expressed in brain. Expressed at moderate
CC       levels in most tissues, except bone marrow.
CC       {ECO:0000269|PubMed:16357137}.
CC   -!- DEVELOPMENTAL STAGE: Expression is cell-cycle regulated, and peaks at
CC       late G2 to early G1 phase (at protein level).
CC       {ECO:0000269|PubMed:16357137}.
CC   -!- INDUCTION: By DNA damage. Increases after UV irradiation, X-ray
CC       irradiation, oxidative stress (H(2)O(2)) or addition of the
CC       chemotherapeutic DNA-damaging agents etoposide, adriamycin, cisplatin
CC       or fluorouracil. {ECO:0000269|PubMed:19412162}.
CC   -!- PTM: Phosphorylation at Ser-278 by ATM following gamma-irradiation
CC       results in its stabilization. {ECO:0000269|PubMed:19412162}.
CC   -!- DISEASE: Intellectual developmental disorder, autosomal recessive 45
CC       (MRT45) [MIM:615979]: A disorder characterized by significantly below
CC       average general intellectual functioning associated with impairments in
CC       adaptive behavior and manifested during the developmental period. MRT45
CC       manifestations include mild to moderate intellectual disability and
CC       dysmorphic features, including coarse facies, broad nasal bridge,
CC       fleshy nares, and thick, prominent lips. {ECO:0000269|PubMed:24623383}.
CC       Note=The disease is caused by variants affecting the gene represented
CC       in this entry.
CC   -!- SIMILARITY: Belongs to the FBXO31 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH12748.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAL55855.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=CAB55929.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="https://atlasgeneticsoncology.org/gene/44280/FBXO31";
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DR   EMBL; AY736035; AAU50679.1; -; mRNA.
DR   EMBL; AF428140; AAQ04213.1; -; mRNA.
DR   EMBL; AF318348; AAL55855.1; ALT_FRAME; mRNA.
DR   EMBL; AC010531; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC012748; AAH12748.1; ALT_INIT; mRNA.
DR   EMBL; AL117444; CAB55929.2; ALT_INIT; mRNA.
DR   CCDS; CCDS32501.1; -. [Q5XUX0-1]
DR   PIR; T17239; T17239.
DR   RefSeq; NP_001269612.1; NM_001282683.1.
DR   RefSeq; NP_079011.3; NM_024735.4. [Q5XUX0-1]
DR   PDB; 5VZT; X-ray; 2.70 A; B/D=66-539.
DR   PDB; 5VZU; X-ray; 2.70 A; B/D=66-539.
DR   PDBsum; 5VZT; -.
DR   PDBsum; 5VZU; -.
DR   AlphaFoldDB; Q5XUX0; -.
DR   SMR; Q5XUX0; -.
DR   BioGRID; 122890; 46.
DR   ComplexPortal; CPX-7971; SCF E3 ubiquitin ligase complex, FBXO31 variant.
DR   CORUM; Q5XUX0; -.
DR   DIP; DIP-60449N; -.
DR   IntAct; Q5XUX0; 22.
DR   STRING; 9606.ENSP00000310841; -.
DR   GlyGen; Q5XUX0; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q5XUX0; -.
DR   PhosphoSitePlus; Q5XUX0; -.
DR   SwissPalm; Q5XUX0; -.
DR   BioMuta; FBXO31; -.
DR   DMDM; 146345419; -.
DR   EPD; Q5XUX0; -.
DR   jPOST; Q5XUX0; -.
DR   MassIVE; Q5XUX0; -.
DR   MaxQB; Q5XUX0; -.
DR   PaxDb; 9606-ENSP00000310841; -.
DR   PeptideAtlas; Q5XUX0; -.
DR   ProteomicsDB; 65845; -. [Q5XUX0-1]
DR   ProteomicsDB; 65846; -. [Q5XUX0-2]
DR   Antibodypedia; 30677; 281 antibodies from 24 providers.
DR   DNASU; 79791; -.
DR   Ensembl; ENST00000311635.12; ENSP00000310841.4; ENSG00000103264.18. [Q5XUX0-1]
DR   GeneID; 79791; -.
DR   KEGG; hsa:79791; -.
DR   MANE-Select; ENST00000311635.12; ENSP00000310841.4; NM_024735.5; NP_079011.3.
DR   UCSC; uc002fjw.5; human. [Q5XUX0-1]
DR   AGR; HGNC:16510; -.
DR   CTD; 79791; -.
DR   DisGeNET; 79791; -.
DR   GeneCards; FBXO31; -.
DR   HGNC; HGNC:16510; FBXO31.
DR   HPA; ENSG00000103264; Tissue enhanced (skeletal).
DR   MalaCards; FBXO31; -.
DR   MIM; 609102; gene.
DR   MIM; 615979; phenotype.
DR   neXtProt; NX_Q5XUX0; -.
DR   OpenTargets; ENSG00000103264; -.
DR   Orphanet; 88616; Autosomal recessive non-syndromic intellectual disability.
DR   PharmGKB; PA28042; -.
DR   VEuPathDB; HostDB:ENSG00000103264; -.
DR   eggNOG; ENOG502QR2A; Eukaryota.
DR   GeneTree; ENSGT00390000001368; -.
DR   HOGENOM; CLU_035961_0_0_1; -.
DR   InParanoid; Q5XUX0; -.
DR   OMA; CCKPEKH; -.
DR   OrthoDB; 5190824at2759; -.
DR   PhylomeDB; Q5XUX0; -.
DR   TreeFam; TF331818; -.
DR   PathwayCommons; Q5XUX0; -.
DR   Reactome; R-HSA-8951664; Neddylation.
DR   Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   SignaLink; Q5XUX0; -.
DR   SIGNOR; Q5XUX0; -.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 79791; 13 hits in 1203 CRISPR screens.
DR   ChiTaRS; FBXO31; human.
DR   GeneWiki; FBXO31; -.
DR   GenomeRNAi; 79791; -.
DR   Pharos; Q5XUX0; Tbio.
DR   PRO; PR:Q5XUX0; -.
DR   Proteomes; UP000005640; Chromosome 16.
DR   RNAct; Q5XUX0; Protein.
DR   Bgee; ENSG00000103264; Expressed in cerebellar hemisphere and 180 other cell types or tissues.
DR   ExpressionAtlas; Q5XUX0; baseline and differential.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
DR   GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:UniProtKB.
DR   GO; GO:0030332; F:cyclin binding; IPI:UniProtKB.
DR   GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; IMP:UniProtKB.
DR   GO; GO:0006974; P:DNA damage response; IDA:UniProtKB.
DR   GO; GO:0031571; P:mitotic G1 DNA damage checkpoint signaling; IMP:UniProtKB.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR   Gene3D; 1.20.1280.50; -; 1.
DR   InterPro; IPR036047; F-box-like_dom_sf.
DR   InterPro; IPR001810; F-box_dom.
DR   InterPro; IPR045048; FBXO31/39.
DR   PANTHER; PTHR10706; F-BOX FAMILY PROTEIN; 1.
DR   PANTHER; PTHR10706:SF130; F-BOX ONLY PROTEIN 31; 1.
DR   Pfam; PF12014; Cyclin_D1_bind; 1.
DR   Pfam; PF12937; F-box-like; 1.
DR   SMART; SM00256; FBOX; 1.
DR   SUPFAM; SSF81383; F-box domain; 1.
DR   PROSITE; PS50181; FBOX; 1.
DR   Genevisible; Q5XUX0; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell cycle; DNA damage;
KW   Intellectual disability; Phosphoprotein; Reference proteome;
KW   Ubl conjugation pathway.
FT   CHAIN           1..539
FT                   /note="F-box only protein 31"
FT                   /id="PRO_0000119921"
FT   DOMAIN          64..110
FT                   /note="F-box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT   REGION          11..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          377..446
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        377..394
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         33
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3TQF0"
FT   MOD_RES         37
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3TQF0"
FT   MOD_RES         278
FT                   /note="Phosphoserine; by ATM"
FT                   /evidence="ECO:0000269|PubMed:19412162"
FT   VAR_SEQ         1..113
FT                   /note="MAVCARLCGVGPSRGCRRRQQRRGPAETAAADSEPDTDPEEERIEASAGVGG
FT                   GLCAGPSPPPPRCSLLELPPELLVEIFASLPGTDLPSLAQVCTKFRRILHTDTIWRRRC
FT                   RE -> MFLVT (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15498874"
FT                   /id="VSP_037469"
FT   MUTAGEN         278
FT                   /note="S->A: Fails to accumulate following
FT                   gamma-irradiation."
FT                   /evidence="ECO:0000269|PubMed:19412162"
FT   MUTAGEN         400
FT                   /note="S->A: No effect following gamma-irradiation."
FT                   /evidence="ECO:0000269|PubMed:19412162"
FT   CONFLICT        138
FT                   /note="L -> V (in Ref. 1; AAU50679)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        281
FT                   /note="D -> E (in Ref. 1; AAU50679)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        466
FT                   /note="C -> S (in Ref. 1; AAU50679)"
FT                   /evidence="ECO:0000305"
FT   HELIX           67..69
FT                   /evidence="ECO:0007829|PDB:5VZT"
FT   HELIX           72..80
FT                   /evidence="ECO:0007829|PDB:5VZT"
FT   TURN            84..86
FT                   /evidence="ECO:0007829|PDB:5VZT"
FT   HELIX           87..91
FT                   /evidence="ECO:0007829|PDB:5VZT"
FT   HELIX           95..100
FT                   /evidence="ECO:0007829|PDB:5VZT"
FT   HELIX           104..115
FT                   /evidence="ECO:0007829|PDB:5VZT"
FT   HELIX           121..126
FT                   /evidence="ECO:0007829|PDB:5VZT"
FT   HELIX           131..137
FT                   /evidence="ECO:0007829|PDB:5VZT"
FT   TURN            138..142
FT                   /evidence="ECO:0007829|PDB:5VZT"
FT   HELIX           143..145
FT                   /evidence="ECO:0007829|PDB:5VZT"
FT   STRAND          147..151
FT                   /evidence="ECO:0007829|PDB:5VZT"
FT   STRAND          160..165
FT                   /evidence="ECO:0007829|PDB:5VZT"
FT   STRAND          168..175
FT                   /evidence="ECO:0007829|PDB:5VZT"
FT   STRAND          187..195
FT                   /evidence="ECO:0007829|PDB:5VZT"
FT   STRAND          203..206
FT                   /evidence="ECO:0007829|PDB:5VZT"
FT   STRAND          209..211
FT                   /evidence="ECO:0007829|PDB:5VZT"
FT   STRAND          214..220
FT                   /evidence="ECO:0007829|PDB:5VZT"
FT   STRAND          222..231
FT                   /evidence="ECO:0007829|PDB:5VZT"
FT   HELIX           233..235
FT                   /evidence="ECO:0007829|PDB:5VZT"
FT   HELIX           242..253
FT                   /evidence="ECO:0007829|PDB:5VZT"
FT   HELIX           258..261
FT                   /evidence="ECO:0007829|PDB:5VZU"
FT   HELIX           264..278
FT                   /evidence="ECO:0007829|PDB:5VZT"
FT   STRAND          280..282
FT                   /evidence="ECO:0007829|PDB:5VZT"
FT   STRAND          285..289
FT                   /evidence="ECO:0007829|PDB:5VZT"
FT   STRAND          296..298
FT                   /evidence="ECO:0007829|PDB:5VZT"
FT   STRAND          303..308
FT                   /evidence="ECO:0007829|PDB:5VZT"
FT   HELIX           310..312
FT                   /evidence="ECO:0007829|PDB:5VZT"
FT   STRAND          314..321
FT                   /evidence="ECO:0007829|PDB:5VZT"
FT   STRAND          323..332
FT                   /evidence="ECO:0007829|PDB:5VZT"
FT   STRAND          335..337
FT                   /evidence="ECO:0007829|PDB:5VZT"
FT   STRAND          341..352
FT                   /evidence="ECO:0007829|PDB:5VZT"
FT   HELIX           357..360
FT                   /evidence="ECO:0007829|PDB:5VZT"
FT   HELIX           363..380
FT                   /evidence="ECO:0007829|PDB:5VZT"
FT   STRAND          453..455
FT                   /evidence="ECO:0007829|PDB:5VZT"
FT   STRAND          464..475
FT                   /evidence="ECO:0007829|PDB:5VZT"
FT   TURN            476..478
FT                   /evidence="ECO:0007829|PDB:5VZT"
FT   STRAND          479..492
FT                   /evidence="ECO:0007829|PDB:5VZT"
FT   STRAND          495..500
FT                   /evidence="ECO:0007829|PDB:5VZT"
FT   HELIX           501..503
FT                   /evidence="ECO:0007829|PDB:5VZT"
FT   STRAND          505..511
FT                   /evidence="ECO:0007829|PDB:5VZT"
FT   HELIX           524..536
FT                   /evidence="ECO:0007829|PDB:5VZT"
SQ   SEQUENCE   539 AA;  60664 MW;  E833D63A361E7381 CRC64;
     MAVCARLCGV GPSRGCRRRQ QRRGPAETAA ADSEPDTDPE EERIEASAGV GGGLCAGPSP
     PPPRCSLLEL PPELLVEIFA SLPGTDLPSL AQVCTKFRRI LHTDTIWRRR CREEYGVCEN
     LRKLEITGVS CRDVYAKLLH RYRHILGLWQ PDIGPYGGLL NVVVDGLFII GWMYLPPHDP
     HVDDPMRFKP LFRIHLMERK AATVECMYGH KGPHHGHIQI VKKDEFSTKC NQTDHHRMSG
     GRQEEFRTWL REEWGRTLED IFHEHMQELI LMKFIYTSQY DNCLTYRRIY LPPSRPDDLI
     KPGLFKGTYG SHGLEIVMLS FHGRRARGTK ITGDPNIPAG QQTVEIDLRH RIQLPDLENQ
     RNFNELSRIV LEVRERVRQE QQEGGHEAGE GRGRQGPRES QPSPAQPRAE APSKGPDGTP
     GEDGGEPGDA VAAAEQPAQC GQGQPFVLPV GVSSRNEDYP RTCRMCFYGT GLIAGHGFTS
     PERTPGVFIL FDEDRFGFVW LELKSFSLYS RVQATFRNAD APSPQAFDEM LKNIQSLTS
//