Full text data of C2CD5
C2CD5
(CDP138, KIAA0528)
[Confidence: low (only semi-automatic identification from reviews)]
C2 domain-containing protein 5 (C2 domain-containing phosphoprotein of 138 kDa)
C2 domain-containing protein 5 (C2 domain-containing phosphoprotein of 138 kDa)
UniProt
Q86YS7
ID C2CD5_HUMAN Reviewed; 1000 AA.
AC Q86YS7; O60280; Q17RY7; Q7Z619; Q86SU3;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-2003, sequence version 1.
DT 22-JAN-2014, entry version 88.
DE RecName: Full=C2 domain-containing protein 5;
DE AltName: Full=C2 domain-containing phosphoprotein of 138 kDa;
GN Name=C2CD5; Synonyms=CDP138, KIAA0528;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9628581; DOI=10.1093/dnares/5.1.31;
RA Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
RA Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. IX.
RT The complete sequences of 100 new cDNA clones from brain which can
RT code for large proteins in vitro.";
RL DNA Res. 5:31-39(1998).
RN [2]
RP SEQUENCE REVISION.
RA Ohara O., Nagase T., Ishikawa K.;
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
RA Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
RA Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
RA Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA Kucherlapati R., Weinstock G., Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Guo J.H., Yu L.;
RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Cerebellum, and Lung carcinoma;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-643, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-601; SER-643 AND
RP SER-852, AND MASS SPECTROMETRY.
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
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-643; SER-659 AND
RP SER-852, AND MASS SPECTROMETRY.
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-317; SER-643 AND
RP SER-852, AND MASS SPECTROMETRY.
RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-643 AND SER-659, AND
RP MASS SPECTROMETRY.
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP FUNCTION, PHOSPHORYLATION AT SER-197 AND SER-200, INTERACTION WITH
RP PHOSPHOLIPIDS, CALCIUM-BINDING, SUBCELLULAR LOCATION, MUTAGENESIS OF
RP ASP-19; ASP-26; ASP-76; ASP-78; ASP-84; SER-197 AND SER-200, AND MASS
RP SEPCTROMETRY.
RX PubMed=21907143; DOI=10.1016/j.cmet.2011.06.015;
RA Xie X., Gong Z., Mansuy-Aubert V., Zhou Q.L., Tatulian S.A., Sehrt D.,
RA Gnad F., Brill L.M., Motamedchaboki K., Chen Y., Czech M.P., Mann M.,
RA Kruger M., Jiang Z.Y.;
RT "C2 domain-containing phosphoprotein CDP138 regulates GLUT4 insertion
RT into the plasma membrane.";
RL Cell Metab. 14:378-389(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-293; SER-295 AND
RP SER-852, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: Required for insulin-stimulated glucose transport and
CC glucose transporter SLC2A4/GLUT4 translocation from intracellular
CC glucose storage vesicle (GSV) to the plasma membrane (PM) in
CC adipocytes. Binds phospholipid membranes in a calcium-dependent
CC manner and is necessary for the optimal membrane fusion between
CC SLC2A4/GLUT4 GSV and the PM.
CC -!- COFACTOR: Binds 2 calcium ions per subunit. The ions are bound to
CC the C2 domains.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane. Cytoplasm,
CC cell cortex. Cell membrane. Cell projection, ruffle.
CC Note=Dynamically associated with GLUT4-containing glucose storage
CC vesicles (GSV) and plasma membrane in response to insulin
CC stimulation.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q86YS7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86YS7-2; Sequence=VSP_028255, VSP_028256;
CC Note=No experimental confirmation available;
CC -!- DOMAIN: The C2 domain binds to calcium and membrane lipids.
CC -!- PTM: Phosphorylated on Ser-197 by active myristoylated kinase
CC AKT2; insulin-stimulated phosphorylation by AKT2 regulates
CC SLC2A4/GLUT4 translocation into the plasma membrane.
CC -!- SIMILARITY: Contains 1 C2 domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA25454.3; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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DR EMBL; AB011100; BAA25454.3; ALT_INIT; mRNA.
DR EMBL; AC053513; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AY166851; AAO17290.1; -; mRNA.
DR EMBL; BC042498; AAH42498.2; -; mRNA.
DR EMBL; BC053885; AAH53885.1; -; mRNA.
DR EMBL; BC117143; AAI17144.1; -; mRNA.
DR PIR; T00072; T00072.
DR RefSeq; NP_001273102.1; NM_001286173.1.
DR RefSeq; NP_001273103.1; NM_001286174.1.
DR RefSeq; NP_001273104.1; NM_001286175.1.
DR RefSeq; NP_001273105.1; NM_001286176.1.
DR RefSeq; NP_001273106.1; NM_001286177.1.
DR RefSeq; NP_055617.1; NM_014802.2.
DR UniGene; Hs.271014; -.
DR ProteinModelPortal; Q86YS7; -.
DR SMR; Q86YS7; 3-125.
DR IntAct; Q86YS7; 2.
DR STRING; 9606.ENSP00000334229; -.
DR PhosphoSite; Q86YS7; -.
DR DMDM; 74750574; -.
DR PaxDb; Q86YS7; -.
DR PRIDE; Q86YS7; -.
DR Ensembl; ENST00000333957; ENSP00000334229; ENSG00000111731.
DR Ensembl; ENST00000396028; ENSP00000379345; ENSG00000111731.
DR GeneID; 9847; -.
DR KEGG; hsa:9847; -.
DR UCSC; uc001rfq.3; human.
DR CTD; 9847; -.
DR GeneCards; GC12M022602; -.
DR HGNC; HGNC:29062; C2CD5.
DR HPA; HPA046194; -.
DR neXtProt; NX_Q86YS7; -.
DR PharmGKB; PA143485515; -.
DR eggNOG; NOG235531; -.
DR HOGENOM; HOG000006746; -.
DR HOVERGEN; HBG081824; -.
DR OrthoDB; EOG715Q38; -.
DR GenomeRNAi; 9847; -.
DR NextBio; 37112; -.
DR ArrayExpress; Q86YS7; -.
DR Bgee; Q86YS7; -.
DR CleanEx; HS_KIAA0528; -.
DR Genevestigator; Q86YS7; -.
DR GO; GO:0005938; C:cell cortex; IDA:UniProtKB.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IDA:UniProtKB.
DR GO; GO:0032587; C:ruffle membrane; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IDA:UniProtKB.
DR GO; GO:0038028; P:insulin receptor signaling pathway via phosphatidylinositol 3-kinase cascade; ISS:UniProtKB.
DR GO; GO:0065002; P:intracellular protein transmembrane transport; IMP:UniProtKB.
DR GO; GO:2001275; P:positive regulation of glucose import in response to insulin stimulus; IEA:Ensembl.
DR GO; GO:0010828; P:positive regulation of glucose transport; ISS:UniProtKB.
DR GO; GO:0090314; P:positive regulation of protein targeting to membrane; IMP:UniProtKB.
DR GO; GO:0031340; P:positive regulation of vesicle fusion; IMP:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; IEA:Ensembl.
DR GO; GO:0006906; P:vesicle fusion; IEA:Ensembl.
DR InterPro; IPR000008; C2_dom.
DR Pfam; PF00168; C2; 1.
DR SMART; SM00239; C2; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR PROSITE; PS50004; C2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell membrane; Cell projection;
KW Complete proteome; Cytoplasm; Cytoplasmic vesicle; Lipid-binding;
KW Membrane; Phosphoprotein; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1 1000 C2 domain-containing protein 5.
FT /FTId=PRO_0000247450.
FT DOMAIN 1 90 C2.
FT CA_BIND 13 27 1; low affinity.
FT CA_BIND 75 86 2; high affinity.
FT MOD_RES 197 197 Phosphoserine; by PKB/AKT2.
FT MOD_RES 200 200 Phosphoserine.
FT MOD_RES 293 293 Phosphoserine.
FT MOD_RES 295 295 Phosphoserine.
FT MOD_RES 317 317 Phosphothreonine.
FT MOD_RES 601 601 Phosphothreonine.
FT MOD_RES 643 643 Phosphoserine.
FT MOD_RES 659 659 Phosphoserine.
FT MOD_RES 852 852 Phosphoserine.
FT VAR_SEQ 268 316 IPFNEDPNPNTHSSGPSTPLKNQTYSFSPSKSYSRQSSSSD
FT TDLSLTPK -> SPLVHPPSHGCRSTHNSPIHTATGSRLTQ
FT NFSVSVPTLIY (in isoform 2).
FT /FTId=VSP_028255.
FT VAR_SEQ 844 845 KA -> KEHLESASSNSGIPAAQRATSVDYSSFADRCSSWI
FT ELIKLKAQTIRRGSIKTT (in isoform 2).
FT /FTId=VSP_028256.
FT MUTAGEN 19 19 D->A: Reduces calcium-binding,
FT phospholipid membrane-binding and
FT insulin-stimulated SLC2A4/GLUT4
FT translocation; when associated with A-26;
FT A-76; A-78 and A-84.
FT MUTAGEN 26 26 D->A: Reduces calcium-binding,
FT phospholipid membrane-binding and
FT insulin-stimulated SLC2A4/GLUT4
FT translocation; when associated with A-19;
FT A-76; A-78 and A-84.
FT MUTAGEN 76 76 D->A: Reduces calcium-binding,
FT phospholipid membrane-binding and
FT insulin-stimulated SLC2A4/GLUT4
FT translocation; when associated with A-19;
FT A-26; A-78 and A-84.
FT MUTAGEN 78 78 D->A: Reduces calcium-binding,
FT phospholipid membrane-binding and
FT insulin-stimulated SLC2A4/GLUT4
FT translocation; when associated with A-19;
FT A-26; A-76 and A-84.
FT MUTAGEN 84 84 D->A: Reduces calcium-binding,
FT phospholipid membrane-binding and
FT insulin-stimulated SLC2A4/GLUT4
FT translocation; when associated with A-19;
FT A-26; A-76 and A-78.
FT MUTAGEN 197 197 S->A: Inhibits insulin-stimulated AKT2-
FT induced phosphorylation, SLC2A4/GLUT4
FT translocation to the cell surface and
FT GSV-PM fusion.
FT MUTAGEN 200 200 S->A: Does not inhibit insulin-stimulated
FT SLC2A4/GLUT4 translocation.
SQ SEQUENCE 1000 AA; 110447 MW; 7C51961F54CBBACD CRC64;
MPGKLKVKIV AGRHLPVMDR ASDLTDAFVE VKFGNTTFKT DVYLKSLNPQ WNSEWFKFEV
DDEDLQDEPL QITVLDHDTY SANDAIGKVY IDIDPLLYSE AATVISGWFP IYDTIHGIRG
EINVVVKVDL FNDLNRFRQS SCGVKFFCTT SIPKCYRAVI IHGFVEELVV NEDPEYQWID
RIRTPRASNE ARQRLISLMS GELQRKIGLK VLEMRGNAVV GYLQCFDLEG ESGLVVRAIG
TACTLDKLSS PAAFLPACNS PSKEMKEIPF NEDPNPNTHS SGPSTPLKNQ TYSFSPSKSY
SRQSSSSDTD LSLTPKTGMG SGSAGKEGGP FKALLRQQTQ SALEQREFPF FTLTAFPPGF
LVHVGGVVSA RSVKLLDRIH NPDEPETRDA WWAEIRQEIK SHAKALGCHA VVGYSESTSI
CEEVCILSAS GTAAVLNPRF LQDGTVEGCL EQRLEENLPT RCGFCHIPYD ELNMPFPAHL
TYCYNCRKQK VPDVLFTTID LPTDATVIGK GCLIQARLCR LKKKAQAEAN ATAISNLLPF
MEYEVHTQLM NKLKLKGMNA LFGLRIQITV GENMLMGLAS ATGVYLAALP TPGGIQIAGK
TPNDGSYEQH ISHMQKKIND TIAKNKELYE INPPEISEEI IGSPIPEPRQ RSRLLRSQSE
SSDEVTELDL SHGKKDAFVL EIDDTDAMED VHSLLTDVPP PSGFYSCNTE IMPGINNWTS
EIQMFTSVRV IRLSSLNLTN QALNKNFNDL CENLLKSLYF KLRSMIPCCL CHVNFTVSLP
EDELIQVTVT AVAITFDKNQ ALQTTKTPVE KSLQRASTDN EELLQFPLEL CSDSLPSHPF
PPAKAMTVEK ASPVGDGNFR NRSAPPCANS TVGVVKMTPL SFIPGAKITK YLGIINMFFI
RETTSLREEG GVSGFLHAFI AEVFAMVRAH VAALGGNAVV SYIMKQCVFM ENPNKNQAQC
LINVSGDAVV FVRESDLEVV SSQQPTTNCQ SSCTEGEVTT
//
ID C2CD5_HUMAN Reviewed; 1000 AA.
AC Q86YS7; O60280; Q17RY7; Q7Z619; Q86SU3;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-2003, sequence version 1.
DT 22-JAN-2014, entry version 88.
DE RecName: Full=C2 domain-containing protein 5;
DE AltName: Full=C2 domain-containing phosphoprotein of 138 kDa;
GN Name=C2CD5; Synonyms=CDP138, KIAA0528;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9628581; DOI=10.1093/dnares/5.1.31;
RA Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
RA Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. IX.
RT The complete sequences of 100 new cDNA clones from brain which can
RT code for large proteins in vitro.";
RL DNA Res. 5:31-39(1998).
RN [2]
RP SEQUENCE REVISION.
RA Ohara O., Nagase T., Ishikawa K.;
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
RA Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
RA Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
RA Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA Kucherlapati R., Weinstock G., Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Guo J.H., Yu L.;
RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Cerebellum, and Lung carcinoma;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-643, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-601; SER-643 AND
RP SER-852, AND MASS SPECTROMETRY.
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
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-643; SER-659 AND
RP SER-852, AND MASS SPECTROMETRY.
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-317; SER-643 AND
RP SER-852, AND MASS SPECTROMETRY.
RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-643 AND SER-659, AND
RP MASS SPECTROMETRY.
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP FUNCTION, PHOSPHORYLATION AT SER-197 AND SER-200, INTERACTION WITH
RP PHOSPHOLIPIDS, CALCIUM-BINDING, SUBCELLULAR LOCATION, MUTAGENESIS OF
RP ASP-19; ASP-26; ASP-76; ASP-78; ASP-84; SER-197 AND SER-200, AND MASS
RP SEPCTROMETRY.
RX PubMed=21907143; DOI=10.1016/j.cmet.2011.06.015;
RA Xie X., Gong Z., Mansuy-Aubert V., Zhou Q.L., Tatulian S.A., Sehrt D.,
RA Gnad F., Brill L.M., Motamedchaboki K., Chen Y., Czech M.P., Mann M.,
RA Kruger M., Jiang Z.Y.;
RT "C2 domain-containing phosphoprotein CDP138 regulates GLUT4 insertion
RT into the plasma membrane.";
RL Cell Metab. 14:378-389(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-293; SER-295 AND
RP SER-852, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: Required for insulin-stimulated glucose transport and
CC glucose transporter SLC2A4/GLUT4 translocation from intracellular
CC glucose storage vesicle (GSV) to the plasma membrane (PM) in
CC adipocytes. Binds phospholipid membranes in a calcium-dependent
CC manner and is necessary for the optimal membrane fusion between
CC SLC2A4/GLUT4 GSV and the PM.
CC -!- COFACTOR: Binds 2 calcium ions per subunit. The ions are bound to
CC the C2 domains.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane. Cytoplasm,
CC cell cortex. Cell membrane. Cell projection, ruffle.
CC Note=Dynamically associated with GLUT4-containing glucose storage
CC vesicles (GSV) and plasma membrane in response to insulin
CC stimulation.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q86YS7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86YS7-2; Sequence=VSP_028255, VSP_028256;
CC Note=No experimental confirmation available;
CC -!- DOMAIN: The C2 domain binds to calcium and membrane lipids.
CC -!- PTM: Phosphorylated on Ser-197 by active myristoylated kinase
CC AKT2; insulin-stimulated phosphorylation by AKT2 regulates
CC SLC2A4/GLUT4 translocation into the plasma membrane.
CC -!- SIMILARITY: Contains 1 C2 domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA25454.3; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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DR EMBL; AB011100; BAA25454.3; ALT_INIT; mRNA.
DR EMBL; AC053513; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AY166851; AAO17290.1; -; mRNA.
DR EMBL; BC042498; AAH42498.2; -; mRNA.
DR EMBL; BC053885; AAH53885.1; -; mRNA.
DR EMBL; BC117143; AAI17144.1; -; mRNA.
DR PIR; T00072; T00072.
DR RefSeq; NP_001273102.1; NM_001286173.1.
DR RefSeq; NP_001273103.1; NM_001286174.1.
DR RefSeq; NP_001273104.1; NM_001286175.1.
DR RefSeq; NP_001273105.1; NM_001286176.1.
DR RefSeq; NP_001273106.1; NM_001286177.1.
DR RefSeq; NP_055617.1; NM_014802.2.
DR UniGene; Hs.271014; -.
DR ProteinModelPortal; Q86YS7; -.
DR SMR; Q86YS7; 3-125.
DR IntAct; Q86YS7; 2.
DR STRING; 9606.ENSP00000334229; -.
DR PhosphoSite; Q86YS7; -.
DR DMDM; 74750574; -.
DR PaxDb; Q86YS7; -.
DR PRIDE; Q86YS7; -.
DR Ensembl; ENST00000333957; ENSP00000334229; ENSG00000111731.
DR Ensembl; ENST00000396028; ENSP00000379345; ENSG00000111731.
DR GeneID; 9847; -.
DR KEGG; hsa:9847; -.
DR UCSC; uc001rfq.3; human.
DR CTD; 9847; -.
DR GeneCards; GC12M022602; -.
DR HGNC; HGNC:29062; C2CD5.
DR HPA; HPA046194; -.
DR neXtProt; NX_Q86YS7; -.
DR PharmGKB; PA143485515; -.
DR eggNOG; NOG235531; -.
DR HOGENOM; HOG000006746; -.
DR HOVERGEN; HBG081824; -.
DR OrthoDB; EOG715Q38; -.
DR GenomeRNAi; 9847; -.
DR NextBio; 37112; -.
DR ArrayExpress; Q86YS7; -.
DR Bgee; Q86YS7; -.
DR CleanEx; HS_KIAA0528; -.
DR Genevestigator; Q86YS7; -.
DR GO; GO:0005938; C:cell cortex; IDA:UniProtKB.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IDA:UniProtKB.
DR GO; GO:0032587; C:ruffle membrane; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IDA:UniProtKB.
DR GO; GO:0038028; P:insulin receptor signaling pathway via phosphatidylinositol 3-kinase cascade; ISS:UniProtKB.
DR GO; GO:0065002; P:intracellular protein transmembrane transport; IMP:UniProtKB.
DR GO; GO:2001275; P:positive regulation of glucose import in response to insulin stimulus; IEA:Ensembl.
DR GO; GO:0010828; P:positive regulation of glucose transport; ISS:UniProtKB.
DR GO; GO:0090314; P:positive regulation of protein targeting to membrane; IMP:UniProtKB.
DR GO; GO:0031340; P:positive regulation of vesicle fusion; IMP:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; IEA:Ensembl.
DR GO; GO:0006906; P:vesicle fusion; IEA:Ensembl.
DR InterPro; IPR000008; C2_dom.
DR Pfam; PF00168; C2; 1.
DR SMART; SM00239; C2; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR PROSITE; PS50004; C2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell membrane; Cell projection;
KW Complete proteome; Cytoplasm; Cytoplasmic vesicle; Lipid-binding;
KW Membrane; Phosphoprotein; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1 1000 C2 domain-containing protein 5.
FT /FTId=PRO_0000247450.
FT DOMAIN 1 90 C2.
FT CA_BIND 13 27 1; low affinity.
FT CA_BIND 75 86 2; high affinity.
FT MOD_RES 197 197 Phosphoserine; by PKB/AKT2.
FT MOD_RES 200 200 Phosphoserine.
FT MOD_RES 293 293 Phosphoserine.
FT MOD_RES 295 295 Phosphoserine.
FT MOD_RES 317 317 Phosphothreonine.
FT MOD_RES 601 601 Phosphothreonine.
FT MOD_RES 643 643 Phosphoserine.
FT MOD_RES 659 659 Phosphoserine.
FT MOD_RES 852 852 Phosphoserine.
FT VAR_SEQ 268 316 IPFNEDPNPNTHSSGPSTPLKNQTYSFSPSKSYSRQSSSSD
FT TDLSLTPK -> SPLVHPPSHGCRSTHNSPIHTATGSRLTQ
FT NFSVSVPTLIY (in isoform 2).
FT /FTId=VSP_028255.
FT VAR_SEQ 844 845 KA -> KEHLESASSNSGIPAAQRATSVDYSSFADRCSSWI
FT ELIKLKAQTIRRGSIKTT (in isoform 2).
FT /FTId=VSP_028256.
FT MUTAGEN 19 19 D->A: Reduces calcium-binding,
FT phospholipid membrane-binding and
FT insulin-stimulated SLC2A4/GLUT4
FT translocation; when associated with A-26;
FT A-76; A-78 and A-84.
FT MUTAGEN 26 26 D->A: Reduces calcium-binding,
FT phospholipid membrane-binding and
FT insulin-stimulated SLC2A4/GLUT4
FT translocation; when associated with A-19;
FT A-76; A-78 and A-84.
FT MUTAGEN 76 76 D->A: Reduces calcium-binding,
FT phospholipid membrane-binding and
FT insulin-stimulated SLC2A4/GLUT4
FT translocation; when associated with A-19;
FT A-26; A-78 and A-84.
FT MUTAGEN 78 78 D->A: Reduces calcium-binding,
FT phospholipid membrane-binding and
FT insulin-stimulated SLC2A4/GLUT4
FT translocation; when associated with A-19;
FT A-26; A-76 and A-84.
FT MUTAGEN 84 84 D->A: Reduces calcium-binding,
FT phospholipid membrane-binding and
FT insulin-stimulated SLC2A4/GLUT4
FT translocation; when associated with A-19;
FT A-26; A-76 and A-78.
FT MUTAGEN 197 197 S->A: Inhibits insulin-stimulated AKT2-
FT induced phosphorylation, SLC2A4/GLUT4
FT translocation to the cell surface and
FT GSV-PM fusion.
FT MUTAGEN 200 200 S->A: Does not inhibit insulin-stimulated
FT SLC2A4/GLUT4 translocation.
SQ SEQUENCE 1000 AA; 110447 MW; 7C51961F54CBBACD CRC64;
MPGKLKVKIV AGRHLPVMDR ASDLTDAFVE VKFGNTTFKT DVYLKSLNPQ WNSEWFKFEV
DDEDLQDEPL QITVLDHDTY SANDAIGKVY IDIDPLLYSE AATVISGWFP IYDTIHGIRG
EINVVVKVDL FNDLNRFRQS SCGVKFFCTT SIPKCYRAVI IHGFVEELVV NEDPEYQWID
RIRTPRASNE ARQRLISLMS GELQRKIGLK VLEMRGNAVV GYLQCFDLEG ESGLVVRAIG
TACTLDKLSS PAAFLPACNS PSKEMKEIPF NEDPNPNTHS SGPSTPLKNQ TYSFSPSKSY
SRQSSSSDTD LSLTPKTGMG SGSAGKEGGP FKALLRQQTQ SALEQREFPF FTLTAFPPGF
LVHVGGVVSA RSVKLLDRIH NPDEPETRDA WWAEIRQEIK SHAKALGCHA VVGYSESTSI
CEEVCILSAS GTAAVLNPRF LQDGTVEGCL EQRLEENLPT RCGFCHIPYD ELNMPFPAHL
TYCYNCRKQK VPDVLFTTID LPTDATVIGK GCLIQARLCR LKKKAQAEAN ATAISNLLPF
MEYEVHTQLM NKLKLKGMNA LFGLRIQITV GENMLMGLAS ATGVYLAALP TPGGIQIAGK
TPNDGSYEQH ISHMQKKIND TIAKNKELYE INPPEISEEI IGSPIPEPRQ RSRLLRSQSE
SSDEVTELDL SHGKKDAFVL EIDDTDAMED VHSLLTDVPP PSGFYSCNTE IMPGINNWTS
EIQMFTSVRV IRLSSLNLTN QALNKNFNDL CENLLKSLYF KLRSMIPCCL CHVNFTVSLP
EDELIQVTVT AVAITFDKNQ ALQTTKTPVE KSLQRASTDN EELLQFPLEL CSDSLPSHPF
PPAKAMTVEK ASPVGDGNFR NRSAPPCANS TVGVVKMTPL SFIPGAKITK YLGIINMFFI
RETTSLREEG GVSGFLHAFI AEVFAMVRAH VAALGGNAVV SYIMKQCVFM ENPNKNQAQC
LINVSGDAVV FVRESDLEVV SSQQPTTNCQ SSCTEGEVTT
//