C2CD5_MOUSE
ID C2CD5_MOUSE Reviewed; 1016 AA.
AC Q7TPS5; Q3TQY6; Q6A052; Q80VA1; Q8C0U3; Q8CID5; Q9CS85;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=C2 domain-containing protein 5;
DE AltName: Full=138 kDa C2 domain-containing phosphoprotein;
GN Name=C2cd5; Synonyms=Cdp138, Kiaa0528;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Fetal brain;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 710-1016 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Egg, Embryo, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 513-1016 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Egg, and Mammary tumor;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304; SER-305; SER-306;
RP SER-657; SER-659; SER-661; SER-662 AND SER-817, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP FUNCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
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 into
RT the plasma membrane.";
RL Cell Metab. 14:378-389(2011).
CC -!- FUNCTION: Required for insulin-stimulated glucose transport and glucose
CC transporter SLC2A4/GLUT4 translocation from intracellular glucose
CC storage vesicle (GSV) to the plasma membrane (PM) in adipocytes. Binds
CC phospholipid membranes in a calcium-dependent manner and is necessary
CC for the optimal membrane fusion between SLC2A4/GLUT4 GSV and the PM.
CC {ECO:0000269|PubMed:21907143}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
CC Note=Binds 3 Ca(2+) ions per C2 domain. {ECO:0000255|PROSITE-
CC ProRule:PRU00041};
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000250}.
CC Cytoplasm, cell cortex {ECO:0000250}. Cell membrane {ECO:0000250}. Cell
CC projection, ruffle {ECO:0000250}. Note=Dynamically associated with
CC GLUT4-containing glucose storage vesicles (GSV) and plasma membrane in
CC response to insulin stimulation. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q7TPS5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7TPS5-2; Sequence=VSP_019992, VSP_019993;
CC Name=3;
CC IsoId=Q7TPS5-3; Sequence=VSP_019991;
CC -!- TISSUE SPECIFICITY: Expressed in liver, muscle and fat.
CC -!- DOMAIN: The C2 domain binds to calcium and membrane lipids.
CC {ECO:0000250}.
CC -!- PTM: Phosphorylated on Ser-197 by active myristoylated kinase AKT2;
CC insulin-stimulated phosphorylation by AKT2 regulates SLC2A4/GLUT4
CC translocation into the plasma membrane. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD32244.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK172966; BAD32244.1; ALT_INIT; mRNA.
DR EMBL; AK017577; BAB30814.1; -; mRNA.
DR EMBL; AK029825; BAC26634.1; -; mRNA.
DR EMBL; AK163233; BAE37246.1; -; mRNA.
DR EMBL; BC027763; AAH27763.1; -; mRNA.
DR EMBL; BC049905; AAH49905.1; -; mRNA.
DR EMBL; BC053913; AAH53913.1; -; mRNA.
DR CCDS; CCDS51952.1; -. [Q7TPS5-1]
DR CCDS; CCDS51953.1; -. [Q7TPS5-2]
DR RefSeq; NP_001103158.1; NM_001109688.2. [Q7TPS5-2]
DR RefSeq; NP_001273507.1; NM_001286578.1. [Q7TPS5-3]
DR RefSeq; NP_083357.2; NM_029081.3. [Q7TPS5-1]
DR RefSeq; NP_084173.1; NM_029897.2.
DR AlphaFoldDB; Q7TPS5; -.
DR SMR; Q7TPS5; -.
DR BioGRID; 216985; 4.
DR STRING; 10090.ENSMUSP00000107388; -.
DR iPTMnet; Q7TPS5; -.
DR PhosphoSitePlus; Q7TPS5; -.
DR SwissPalm; Q7TPS5; -.
DR EPD; Q7TPS5; -.
DR jPOST; Q7TPS5; -.
DR MaxQB; Q7TPS5; -.
DR PaxDb; Q7TPS5; -.
DR PeptideAtlas; Q7TPS5; -.
DR PRIDE; Q7TPS5; -.
DR ProteomicsDB; 265465; -. [Q7TPS5-1]
DR ProteomicsDB; 265466; -. [Q7TPS5-2]
DR ProteomicsDB; 265467; -. [Q7TPS5-3]
DR Antibodypedia; 24138; 58 antibodies from 19 providers.
DR DNASU; 74741; -.
DR Ensembl; ENSMUST00000087485; ENSMUSP00000084758; ENSMUSG00000030279. [Q7TPS5-2]
DR Ensembl; ENSMUST00000111758; ENSMUSP00000107388; ENSMUSG00000030279. [Q7TPS5-2]
DR Ensembl; ENSMUST00000203187; ENSMUSP00000145373; ENSMUSG00000030279. [Q7TPS5-1]
DR GeneID; 74741; -.
DR KEGG; mmu:74741; -.
DR UCSC; uc009epx.3; mouse. [Q7TPS5-2]
DR UCSC; uc009epy.3; mouse. [Q7TPS5-1]
DR CTD; 9847; -.
DR MGI; MGI:1921991; C2cd5.
DR VEuPathDB; HostDB:ENSMUSG00000030279; -.
DR eggNOG; KOG1031; Eukaryota.
DR GeneTree; ENSGT00390000000212; -.
DR InParanoid; Q7TPS5; -.
DR OrthoDB; 266134at2759; -.
DR PhylomeDB; Q7TPS5; -.
DR TreeFam; TF323431; -.
DR BioGRID-ORCS; 74741; 6 hits in 72 CRISPR screens.
DR ChiTaRS; C2cd5; mouse.
DR PRO; PR:Q7TPS5; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q7TPS5; protein.
DR Bgee; ENSMUSG00000030279; Expressed in secondary oocyte and 227 other tissues.
DR ExpressionAtlas; Q7TPS5; baseline and differential.
DR Genevisible; Q7TPS5; MM.
DR GO; GO:0005938; C:cell cortex; ISS:UniProtKB.
DR GO; GO:0034451; C:centriolar satellite; ISO:MGI.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0032587; C:ruffle membrane; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IDA:MGI.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; ISS:UniProtKB.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IDA:UniProtKB.
DR GO; GO:0038028; P:insulin receptor signaling pathway via phosphatidylinositol 3-kinase; IMP:UniProtKB.
DR GO; GO:0065002; P:intracellular protein transmembrane transport; ISS:UniProtKB.
DR GO; GO:0046326; P:positive regulation of glucose import; IMP:MGI.
DR GO; GO:0010828; P:positive regulation of glucose transmembrane transport; IMP:UniProtKB.
DR GO; GO:0090314; P:positive regulation of protein targeting to membrane; ISS:UniProtKB.
DR GO; GO:0031340; P:positive regulation of vesicle fusion; IMP:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; IMP:MGI.
DR GO; GO:0006906; P:vesicle fusion; IMP:MGI.
DR CDD; cd08688; C2_KIAA0528-like; 1.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR037785; C2_C2CD5.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR038983; C2CD5.
DR PANTHER; PTHR37412; PTHR37412; 1.
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; Cytoplasm;
KW Cytoplasmic vesicle; Lipid-binding; Membrane; Metal-binding;
KW Phosphoprotein; Protein transport; Reference proteome; Transport.
FT CHAIN 1..1016
FT /note="C2 domain-containing protein 5"
FT /id="PRO_0000247451"
FT DOMAIN 1..109
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 265..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 636..668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..668
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 19
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 19
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 26
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 76
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 76
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 78
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 78
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 78
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 81
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 84
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 84
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT MOD_RES 197
FT /note="Phosphoserine; by PKB/AKT2"
FT /evidence="ECO:0000250|UniProtKB:Q86YS7"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86YS7"
FT MOD_RES 260
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86YS7"
FT MOD_RES 293
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86YS7"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86YS7"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 305
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 306
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 317
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q86YS7"
FT MOD_RES 323
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86YS7"
FT MOD_RES 601
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q86YS7"
FT MOD_RES 643
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86YS7"
FT MOD_RES 657
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 659
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 661
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 662
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 666
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q86YS7"
FT MOD_RES 671
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86YS7"
FT MOD_RES 817
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 869
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86YS7"
FT VAR_SEQ 1..198
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019991"
FT VAR_SEQ 268..316
FT /note="IPFNEDPNPNTHSSGPSTPLKNQTYSFSPSKSYSRQSSSSDTDLSLTPK ->
FT SPLVHPPSHGCRSTHNSPIHTATGSRLTQNFSVSVPTLIY (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15368895,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072"
FT /id="VSP_019992"
FT VAR_SEQ 845..861
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15368895,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072"
FT /id="VSP_019993"
FT CONFLICT 11
FT /note="A -> S (in Ref. 2; BAC26634)"
FT /evidence="ECO:0000305"
FT CONFLICT 590
FT /note="P -> T (in Ref. 2; BAC26634)"
FT /evidence="ECO:0000305"
FT CONFLICT 632
FT /note="T -> S (in Ref. 1; BAD32244 and 3; AAH27763/
FT AAH49905)"
FT /evidence="ECO:0000305"
FT CONFLICT 793
FT /note="A -> V (in Ref. 3; AAH53913)"
FT /evidence="ECO:0000305"
FT CONFLICT 868
FT /note="A -> T (in Ref. 2; BAB30814)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1016 AA; 111664 MW; A1E3614203DFCD03 CRC64;
MPGKLKVKIV AGRHLPVMDR ASDLTDAFVE VKFGNTTFKT DVYLKSLNPQ WNSEWFKFEV
DDEDLQDEPL QITVLDHDTY SANDAIGKVY IDIDPLLYSE AATVISGWFP IYDTIHGIRG
EINVVVKVDL FNDSNRFRQS SCGVKFFCTT SIPKCYRAVV IHGFVEELVV NEDPEYQWID
RIRTPRASNE ARQRLISLMS GELQRKIGLK VLEMRGNAVV GYLQCFDLEG ESGLVVRAIG
TACTLDKLSS PAAFLPACSS PSRELKEIPF NEDPNPNTHS SGPSTPLKNQ TYSFSPSKSY
SRQSSSSDTD LSLTPKTGMG SGSAGKEGGP FKALLRQQTQ SALEQREFPF LTLTAFPPGL
LVHVGGVVSA RSVKLLDRIH NPDEPETRDA WWAEIRQEIK SHAKALGCHA VVGYSESTSI
CEEVCILSAS GTAAVLNPRF LQEGTVEGCL EQRIEENLPV GCGFCHIPYD ELNMPFPAHL
TYCYNCRKQK VPDVLFTTID LPTDAVVVGK GCLIQARLCR LKKKAQAEAN ATAISNLLPF
MEYEVHTQLM NKLKLKGMNA LFGLRIQITV GETMLMGLAS ATGVYLAALP TPGGIQIAGK
TPNDGSYEQH ISHMQKRIND TIAKNKELYE ITPPEVSEEM IGSPIPEPRQ RSRLLRSQSE
SSDEVTELDL SHGKKDAFVL EIDDTDAMED VHSLLTDAPP PSGFYSCNTE IMPGINNWTS
EIQMFTSVRV VRLSSLNLTN QALNKNFNGL CENLLKSLYF KLRSMTPCCL CHVNFTVSLP
EDELIQVTVT AVAITFDKNQ ALQTTKPHVE KSLQRASTDN EELLQFPLEL CSDSLPPHPF
PAAKEHLESA NSNSGIPAAQ RAVTVEKASA MGDGNFRNRS APPCASPTVG VVKMTPLSFI
PGAKITKYLG IINMFFIRET TSLREEGGVS GFLHAFIAEV FAMVRAHVAA LGGNAVVSYI
MKQCVFMENP SKNQAQCLIN VSGDAVVFVR DSDLEVMSSQ QPAANCQPSC TGEVTT
