CPNE6_HUMAN
ID CPNE6_HUMAN Reviewed; 557 AA.
AC O95741; B2RAG6; B7Z1M3; D3DS55; F5GXN1; Q53HA6; Q8WVG1;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 3.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Copine-6 {ECO:0000305};
DE AltName: Full=Copine VI {ECO:0000250|UniProtKB:Q99829, ECO:0000312|HGNC:HGNC:2319};
DE AltName: Full=Neuronal-copine {ECO:0000303|PubMed:9645480};
DE Short=N-copine {ECO:0000303|PubMed:9645480};
GN Name=CPNE6 {ECO:0000312|HGNC:HGNC:2319};
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=Brain;
RX PubMed=9645480; DOI=10.1016/s0014-5793(98)00497-9;
RA Nakayama T., Yaoi T., Yasui M., Kuwajima G.;
RT "N-copine: a novel two C2-domain-containing protein with neuronal activity-
RT regulated expression.";
RL FEBS Lett. 428:80-84(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [7]
RP TISSUE SPECIFICITY.
RX PubMed=10403379; DOI=10.1016/s0014-5793(99)00700-0;
RA Nakayama T., Yaoi T., Kuwajima G., Yoshie O., Sakata T.;
RT "Ca2(+)-dependent interaction of N-copine, a member of the two C2 domain
RT protein family, with OS-9, the product of a gene frequently amplified in
RT osteosarcoma.";
RL FEBS Lett. 453:77-80(1999).
RN [8]
RP INTERACTION WITH NECAB1.
RX PubMed=12044471; DOI=10.1016/s0306-4522(02)00063-5;
RA Sugita S., Ho A., Suedhof T.C.;
RT "NECABs: a family of neuronal Ca(2+)-binding proteins with an unusual
RT domain structure and a restricted expression pattern.";
RL Neuroscience 112:51-63(2002).
RN [9]
RP TISSUE SPECIFICITY.
RX PubMed=12949241; DOI=10.1189/jlb.0203083;
RA Cowland J.B., Carter D., Bjerregaard M.D., Johnsen A.H., Borregaard N.,
RA Lollike K.;
RT "Tissue expression of copines and isolation of copines I and III from the
RT cytosol of human neutrophils.";
RL J. Leukoc. Biol. 74:379-388(2003).
RN [10]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=23999003; DOI=10.1016/j.jdermsci.2013.07.010;
RA Yoo J.C., Lim T.Y., Park J.S., Hah Y.S., Park N., Hong S.G., Park J.Y.,
RA Yoon T.J.;
RT "SYT14L, especially its C2 domain, is involved in regulating melanocyte
RT differentiation.";
RL J. Dermatol. Sci. 72:246-251(2013).
CC -!- FUNCTION: Calcium-dependent phospholipid-binding protein that plays a
CC role in calcium-mediated intracellular processes. Binds phospholipid
CC membranes in a calcium-dependent manner (By similarity). Plays a role
CC in dendrite formation by melanocytes (PubMed:23999003).
CC {ECO:0000250|UniProtKB:Q9Z140, ECO:0000269|PubMed:23999003}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
CC -!- SUBUNIT: Interacts (via second C2 domain) with OS9 (via C-terminus);
CC this interaction occurs in a calcium-dependent manner in vitro (By
CC similarity). May interact with NECAB1 (PubMed:12044471).
CC {ECO:0000250|UniProtKB:Q9Z140, ECO:0000269|PubMed:12044471}.
CC -!- INTERACTION:
CC O95741; P50222: MEOX2; NbExp=3; IntAct=EBI-719005, EBI-748397;
CC O95741-2; O95994: AGR2; NbExp=5; IntAct=EBI-13312079, EBI-712648;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Z140}. Cell
CC membrane {ECO:0000250|UniProtKB:Q9Z140}. Endosome
CC {ECO:0000250|UniProtKB:Q9Z140}. Cytoplasmic vesicle, clathrin-coated
CC vesicle {ECO:0000250|UniProtKB:Q9Z140}. Perikaryon
CC {ECO:0000250|UniProtKB:Q9Z140}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:Q9Z140}. Note=Mainly cytoplasmic in absence of
CC calcium. Associated predominantly with membranes in presence of
CC calcium. Translocates to the cell membrane in a calcium-dependent
CC manner. Colocalized with transferrin in intracellular clathrin-coated
CC membrane vesicles in a calcium-dependent manner.
CC {ECO:0000250|UniProtKB:Q9Z140}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O95741-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O95741-2; Sequence=VSP_054806;
CC -!- TISSUE SPECIFICITY: Widely expressed in the brain (PubMed:9645480,
CC PubMed:10403379, PubMed:12949241). Expressed weakly in the kidney,
CC liver and fetal heart (PubMed:12949241). Expressed in melanocytes
CC (PubMed:23999003). {ECO:0000269|PubMed:10403379,
CC ECO:0000269|PubMed:12949241, ECO:0000269|PubMed:23999003,
CC ECO:0000269|PubMed:9645480}.
CC -!- DOMAIN: The C2 domain 1 binds phospholipids in a calcium-independent
CC manner and is not necessary for calcium-mediated translocation and
CC association to the plasma membrane. The C2 domain 2 binds phospholipids
CC in a calcium-dependent manner and is necessary for calcium-mediated
CC translocation and association to the plasma membrane. The linker region
CC contributes to the calcium-dependent translocation and association to
CC the plasma membrane. The VWFA domain is necessary for association with
CC intracellular clathrin-coated vesicles in a calcium-dependent manner.
CC {ECO:0000250|UniProtKB:Q9Z140}.
CC -!- SIMILARITY: Belongs to the copine family. {ECO:0000305}.
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DR EMBL; AB009288; BAA75899.1; -; mRNA.
DR EMBL; AK222675; BAD96395.1; -; mRNA.
DR EMBL; AK314182; BAG36863.1; -; mRNA.
DR EMBL; AK293655; BAH11559.1; -; mRNA.
DR EMBL; AL136295; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471078; EAW66119.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW66120.1; -; Genomic_DNA.
DR EMBL; BC018046; AAH18046.1; -; mRNA.
DR CCDS; CCDS61413.1; -. [O95741-2]
DR CCDS; CCDS9607.1; -. [O95741-1]
DR RefSeq; NP_001267487.1; NM_001280558.1. [O95741-2]
DR RefSeq; NP_006023.1; NM_006032.3. [O95741-1]
DR RefSeq; XP_005268273.1; XM_005268216.1.
DR AlphaFoldDB; O95741; -.
DR SMR; O95741; -.
DR BioGRID; 114763; 16.
DR IntAct; O95741; 15.
DR MINT; O95741; -.
DR STRING; 9606.ENSP00000440077; -.
DR iPTMnet; O95741; -.
DR PhosphoSitePlus; O95741; -.
DR BioMuta; CPNE6; -.
DR EPD; O95741; -.
DR jPOST; O95741; -.
DR MassIVE; O95741; -.
DR MaxQB; O95741; -.
DR PaxDb; O95741; -.
DR PeptideAtlas; O95741; -.
DR PRIDE; O95741; -.
DR ProteomicsDB; 24474; -.
DR ProteomicsDB; 51017; -. [O95741-1]
DR Antibodypedia; 22599; 169 antibodies from 26 providers.
DR DNASU; 9362; -.
DR Ensembl; ENST00000397016.6; ENSP00000380211.2; ENSG00000100884.10. [O95741-1]
DR Ensembl; ENST00000537691.5; ENSP00000440077.1; ENSG00000100884.10. [O95741-2]
DR Ensembl; ENST00000645359.1; ENSP00000494138.1; ENSG00000285221.1. [O95741-2]
DR Ensembl; ENST00000647071.1; ENSP00000494513.1; ENSG00000285221.1. [O95741-1]
DR Ensembl; ENST00000689861.1; ENSP00000510387.1; ENSG00000100884.10. [O95741-1]
DR GeneID; 9362; -.
DR KEGG; hsa:9362; -.
DR MANE-Select; ENST00000689861.1; ENSP00000510387.1; NM_006032.4; NP_006023.1.
DR UCSC; uc010tnv.4; human. [O95741-1]
DR CTD; 9362; -.
DR GeneCards; CPNE6; -.
DR HGNC; HGNC:2319; CPNE6.
DR HPA; ENSG00000100884; Tissue enhanced (brain, retina).
DR MIM; 605688; gene.
DR neXtProt; NX_O95741; -.
DR OpenTargets; ENSG00000100884; -.
DR PharmGKB; PA26836; -.
DR VEuPathDB; HostDB:ENSG00000100884; -.
DR eggNOG; KOG1327; Eukaryota.
DR GeneTree; ENSGT00940000161567; -.
DR HOGENOM; CLU_020452_4_0_1; -.
DR InParanoid; O95741; -.
DR OMA; PLRCPQG; -.
DR OrthoDB; 1067545at2759; -.
DR PhylomeDB; O95741; -.
DR TreeFam; TF316419; -.
DR PathwayCommons; O95741; -.
DR Reactome; R-HSA-1483206; Glycerophospholipid biosynthesis.
DR SignaLink; O95741; -.
DR BioGRID-ORCS; 9362; 15 hits in 1067 CRISPR screens.
DR GeneWiki; CPNE6; -.
DR GenomeRNAi; 9362; -.
DR Pharos; O95741; Tbio.
DR PRO; PR:O95741; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; O95741; protein.
DR Bgee; ENSG00000100884; Expressed in temporal lobe and 91 other tissues.
DR ExpressionAtlas; O95741; baseline and differential.
DR Genevisible; O95741; HS.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0030136; C:clathrin-coated vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; TAS:ProtInc.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IBA:GO_Central.
DR GO; GO:0001786; F:phosphatidylserine binding; ISS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0071277; P:cellular response to calcium ion; IBA:GO_Central.
DR GO; GO:1903861; P:positive regulation of dendrite extension; IDA:UniProtKB.
DR CDD; cd04047; C2B_Copine; 1.
DR CDD; cd01459; vWA_copine_like; 1.
DR Gene3D; 2.60.40.150; -; 2.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR037768; C2B_Copine.
DR InterPro; IPR045052; Copine.
DR InterPro; IPR010734; Copine_C.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR10857; PTHR10857; 1.
DR Pfam; PF00168; C2; 2.
DR Pfam; PF07002; Copine; 1.
DR SMART; SM00239; C2; 2.
DR SMART; SM00327; VWA; 1.
DR SUPFAM; SSF49562; SSF49562; 2.
DR SUPFAM; SSF53300; SSF53300; 1.
DR PROSITE; PS50004; C2; 2.
DR PROSITE; PS50234; VWFA; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell membrane; Cell projection; Cytoplasm;
KW Cytoplasmic vesicle; Differentiation; Endosome; Membrane; Metal-binding;
KW Reference proteome; Repeat.
FT CHAIN 1..557
FT /note="Copine-6"
FT /id="PRO_0000144845"
FT DOMAIN 2..127
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 134..263
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 306..526
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT REGION 244..303
FT /note="Linker region"
FT /evidence="ECO:0000250|UniProtKB:Q9Z140"
FT BINDING 167
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 167
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 173
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 229
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 229
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 231
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 231
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 237
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT VAR_SEQ 1
FT /note="M -> MAFKEHGKITSCCIPGPINSSRAGAGAGASGWSSKGVRARAREPERG
FT APDREPSDM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054806"
FT CONFLICT 13
FT /note="P -> Q (in Ref. 6; AAH18046)"
FT /evidence="ECO:0000305"
FT CONFLICT 87
FT /note="L -> V (in Ref. 6; AAH18046)"
FT /evidence="ECO:0000305"
FT CONFLICT 198
FT /note="N -> S (in Ref. 2; BAH11559)"
FT /evidence="ECO:0000305"
FT CONFLICT 331
FT /note="P -> H (in Ref. 3; BAD96395)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 557 AA; 61991 MW; CA1ECA3560926FC2 CRC64;
MSDPEMGWVP EPPTMTLGAS RVELRVSCHG LLDRDTLTKP HPCVLLKLYS DEQWVEVERT
EVLRSCSSPV FSRVLALEYF FEEKQPLQFH VFDAEDGATS PRNDTFLGST ECTLGQIVSQ
TKVTKPLLLK NGKTAGKSTI TIVAEEVSGT NDYVQLTFRA YKLDNKDLFS KSDPFMEIYK
TNEDQSDQLV WRTEVVKNNL NPSWEPFRLS LHSLCSCDVH RPLKFLVYDY DSSGKHDFIG
EFTSTFQEMQ EGTANPGQEM QWDCINPKYR DKKKNYKSSG TVVLAQCTVE KVHTFLDYIM
GGCQISFTVA IDFTASNGDP RSSQSLHCLS PRQPNHYLQA LRAVGGICQD YDSDKRFPAF
GFGARIPPNF EVSHDFAINF DPENPECEEI SGVIASYRRC LPQIQLYGPT NVAPIINRVA
EPAQREQSTG QATKYSVLLV LTDGVVSDMA ETRTAIVRAS RLPMSIIIVG VGNADFSDMR
LLDGDDGPLR CPRGVPAARD IVQFVPFRDF KDAAPSALAK CVLAEVPRQV VEYYASQGIS
PGAPRPCTLA TTPSPSP
