CAVN2_HUMAN
ID CAVN2_HUMAN Reviewed; 425 AA.
AC O95810;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Caveolae-associated protein 2 {ECO:0000312|HGNC:HGNC:10690};
DE AltName: Full=Cavin-2;
DE AltName: Full=PS-p68;
DE AltName: Full=Phosphatidylserine-binding protein;
DE AltName: Full=Serum deprivation-response protein;
GN Name=CAVIN2 {ECO:0000312|HGNC:HGNC:10690};
GN Synonyms=SDPR {ECO:0000312|EMBL:AAD17795.1};
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] {ECO:0000305, ECO:0000312|EMBL:AAD17795.1}
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP INDUCTION, AND PHOSPHOLIPID-BINDING.
RX PubMed=10191091; DOI=10.1006/geno.1998.5733;
RA Gustincich S., Vatta P., Goruppi S., Wolf M., Saccone S., Della Valle G.,
RA Baggiolini M., Schneider C.;
RT "The human serum deprivation response gene (SDPR) maps to 2q32-q33 and
RT codes for a phosphatidylserine-binding protein.";
RL Genomics 57:120-129(1999).
RN [2] {ECO:0000312|EMBL:AAY24078.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3] {ECO:0000312|EMBL:AAH16475.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung {ECO:0000312|EMBL:AAH16475.1};
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 PROTEIN SEQUENCE OF 2-10; 49-64; 92-99; 103-113 AND 157-173, CLEAVAGE OF
RP INITIATOR METHIONINE, ACETYLATION AT GLY-2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Platelet;
RA Bienvenut W.V., Claeys D.;
RL Submitted (NOV-2005) to UniProtKB.
RN [5] {ECO:0000305, ECO:0000312|EMBL:AAD17795.1}
RP PROTEIN SEQUENCE OF 80-109; 133-157 AND 256-275, SUBCELLULAR LOCATION,
RP PHOSPHORYLATION, AND PHOSPHOLIPID-BINDING.
RX PubMed=2390065; DOI=10.1042/bj2690729;
RA Burgener R., Wolf M., Ganz T., Baggiolini M.;
RT "Purification and characterization of a major phosphatidylserine-binding
RT phosphoprotein from human platelets.";
RL Biochem. J. 269:729-734(1990).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-293, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using sequential
RT IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [7]
RP INTERACTION WITH CAVIN4.
RX PubMed=18332105; DOI=10.1128/mcb.02186-07;
RA Ogata T., Ueyama T., Isodono K., Tagawa M., Takehara N., Kawashima T.,
RA Harada K., Takahashi T., Shioi T., Matsubara H., Oh H.;
RT "MURC, a muscle-restricted coiled-coil protein that modulates the Rho/ROCK
RT pathway, induces cardiac dysfunction and conduction disturbance.";
RL Mol. Cell. Biol. 28:3424-3436(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-293, 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 [9]
RP SUBCELLULAR LOCATION, DOMAIN LEUCINE ZIPPER, AND MUTAGENESIS OF LEU-86;
RP ILE-93 AND LEU-100.
RX PubMed=19262564; DOI=10.1038/emboj.2009.46;
RA McMahon K.A., Zajicek H., Li W.P., Peyton M.J., Minna J.D., Hernandez V.J.,
RA Luby-Phelps K., Anderson R.G.;
RT "SRBC/cavin-3 is a caveolin adapter protein that regulates caveolae
RT function.";
RL EMBO J. 28:1001-1015(2009).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CAVIN1.
RX PubMed=19525939; DOI=10.1038/ncb1887;
RA Hansen C.G., Bright N.A., Howard G., Nichols B.J.;
RT "SDPR induces membrane curvature and functions in the formation of
RT caveolae.";
RL Nat. Cell Biol. 11:807-814(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288 AND SER-293, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35; THR-196; THR-199;
RP SER-203; SER-204; SER-218; SER-287 AND SER-288, AND IDENTIFICATION BY MASS
RP 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 [13]
RP INTERACTION WITH CAVIN1; CAVIN4 AND CAV3.
RX PubMed=24567387; DOI=10.1073/pnas.1315359111;
RA Ogata T., Naito D., Nakanishi N., Hayashi Y.K., Taniguchi T., Miyagawa K.,
RA Hamaoka T., Maruyama N., Matoba S., Ikeda K., Yamada H., Oh H., Ueyama T.;
RT "MURC/Cavin-4 facilitates recruitment of ERK to caveolae and concentric
RT cardiac hypertrophy induced by alpha1-adrenergic receptors.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:3811-3816(2014).
RN [14]
RP REVIEW.
RX PubMed=26614875; DOI=10.1016/bs.ircmb.2015.07.009;
RA Nassar Z.D., Parat M.O.;
RT "Cavin family: new players in the biology of caveolae.";
RL Int. Rev. Cell Mol. Biol. 320:235-305(2015).
CC -!- FUNCTION: Plays an important role in caveolar biogenesis and
CC morphology. Regulates caveolae morphology by inducing membrane
CC curvature within caveolae (PubMed:19525939). Plays a role in caveola
CC formation in a tissue-specific manner. Required for the formation of
CC caveolae in the lung and fat endothelia but not in the heart
CC endothelia. Negatively regulates the size or stability of CAVIN
CC complexes in the lung endothelial cells. May play a role in targeting
CC PRKCA to caveolae (By similarity). {ECO:0000250|UniProtKB:Q66H98,
CC ECO:0000269|PubMed:19525939}.
CC -!- SUBUNIT: Component of the CAVIN complex composed of CAVIN1, CAVIN2,
CC CAVIN3 and CAVIN4. Binds to PRKCA in the presence of phosphatidylserine
CC (By similarity). Interacts with CAVIN4; this augments the
CC transactivation of NPPA by CAVIN4 (PubMed:18332105, PubMed:24567387).
CC Interacts with CAVIN1 (PubMed:19525939, PubMed:24567387). Interacts
CC with CAV3 (PubMed:24567387). {ECO:0000250|UniProtKB:Q63918,
CC ECO:0000250|UniProtKB:Q66H98, ECO:0000269|PubMed:18332105,
CC ECO:0000269|PubMed:19525939, ECO:0000269|PubMed:24567387}.
CC -!- INTERACTION:
CC O95810; Q9NQ94-2: A1CF; NbExp=3; IntAct=EBI-742141, EBI-10311892;
CC O95810; Q03135: CAV1; NbExp=6; IntAct=EBI-742141, EBI-603614;
CC O95810; Q6NZI2: CAVIN1; NbExp=6; IntAct=EBI-742141, EBI-2559016;
CC O95810; Q96EZ8: MCRS1; NbExp=3; IntAct=EBI-742141, EBI-348259;
CC O95810; P08567: PLEK; NbExp=4; IntAct=EBI-742141, EBI-2565501;
CC O95810; Q96S99: PLEKHF1; NbExp=3; IntAct=EBI-742141, EBI-745767;
CC O95810; O75865-2: TRAPPC6A; NbExp=3; IntAct=EBI-742141, EBI-8451480;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:10191091,
CC ECO:0000269|PubMed:2390065}. Membrane, caveola
CC {ECO:0000269|PubMed:19262564, ECO:0000269|PubMed:19525939}.
CC Note=Localizes in the caveolae in a caveolin-dependent manner.
CC {ECO:0000269|PubMed:19262564}.
CC -!- TISSUE SPECIFICITY: Highly expressed in heart and lung, and expressed
CC at lower levels in brain, kidney, liver, pancreas, placenta, and
CC skeletal muscle. {ECO:0000269|PubMed:10191091}.
CC -!- INDUCTION: Up-regulated in asyncronously growing fibroblasts following
CC serum deprivation but not following contact inhibition. Down-regulated
CC during synchronous cell cycle re-entry. {ECO:0000269|PubMed:10191091}.
CC -!- DOMAIN: The leucine-zipper domain is essential for its localization in
CC the caveolae. {ECO:0000269|PubMed:19262564}.
CC -!- PTM: Phosphorylated on Ser residues. {ECO:0000269|PubMed:2390065}.
CC -!- MISCELLANEOUS: Binds phosphatidylserine (PS) in a calcium-independent
CC manner. PS-binding is inhibited by phosphotidic acid and
CC phosphatidylinositol. Does not bind phosphatidylcholine.
CC -!- SIMILARITY: Belongs to the CAVIN family. {ECO:0000305}.
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DR EMBL; AF085481; AAD17795.1; -; mRNA.
DR EMBL; AC098872; AAY24078.1; -; Genomic_DNA.
DR EMBL; BC016475; AAH16475.1; -; mRNA.
DR CCDS; CCDS2313.1; -.
DR RefSeq; NP_004648.1; NM_004657.5.
DR AlphaFoldDB; O95810; -.
DR SMR; O95810; -.
DR BioGRID; 114016; 22.
DR DIP; DIP-56943N; -.
DR IntAct; O95810; 20.
DR MINT; O95810; -.
DR STRING; 9606.ENSP00000305675; -.
DR CarbonylDB; O95810; -.
DR iPTMnet; O95810; -.
DR PhosphoSitePlus; O95810; -.
DR SwissPalm; O95810; -.
DR BioMuta; CAVIN2; -.
DR OGP; O95810; -.
DR EPD; O95810; -.
DR jPOST; O95810; -.
DR MassIVE; O95810; -.
DR MaxQB; O95810; -.
DR PaxDb; O95810; -.
DR PeptideAtlas; O95810; -.
DR PRIDE; O95810; -.
DR ProteomicsDB; 51062; -.
DR TopDownProteomics; O95810; -.
DR Antibodypedia; 34051; 129 antibodies from 27 providers.
DR DNASU; 8436; -.
DR Ensembl; ENST00000304141.5; ENSP00000305675.4; ENSG00000168497.5.
DR GeneID; 8436; -.
DR KEGG; hsa:8436; -.
DR MANE-Select; ENST00000304141.5; ENSP00000305675.4; NM_004657.6; NP_004648.1.
DR UCSC; uc002utb.4; human.
DR CTD; 8436; -.
DR DisGeNET; 8436; -.
DR GeneCards; CAVIN2; -.
DR HGNC; HGNC:10690; CAVIN2.
DR HPA; ENSG00000168497; Tissue enhanced (adipose).
DR MIM; 606728; gene.
DR neXtProt; NX_O95810; -.
DR OpenTargets; ENSG00000168497; -.
DR PharmGKB; PA35615; -.
DR VEuPathDB; HostDB:ENSG00000168497; -.
DR eggNOG; ENOG502QQCA; Eukaryota.
DR GeneTree; ENSGT00950000182910; -.
DR HOGENOM; CLU_039470_1_0_1; -.
DR InParanoid; O95810; -.
DR OMA; QMPNDQE; -.
DR OrthoDB; 858587at2759; -.
DR PhylomeDB; O95810; -.
DR TreeFam; TF331031; -.
DR PathwayCommons; O95810; -.
DR SignaLink; O95810; -.
DR BioGRID-ORCS; 8436; 11 hits in 1074 CRISPR screens.
DR ChiTaRS; SDPR; human.
DR GeneWiki; SDPR; -.
DR GenomeRNAi; 8436; -.
DR Pharos; O95810; Tbio.
DR PRO; PR:O95810; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; O95810; protein.
DR Bgee; ENSG00000168497; Expressed in monocyte and 170 other tissues.
DR Genevisible; O95810; HS.
DR GO; GO:0005901; C:caveola; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0045121; C:membrane raft; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0001786; F:phosphatidylserine binding; IDA:UniProtKB.
DR GO; GO:0005543; F:phospholipid binding; TAS:ProtInc.
DR GO; GO:0005080; F:protein kinase C binding; IBA:GO_Central.
DR GO; GO:0097320; P:plasma membrane tubulation; IDA:UniProtKB.
DR InterPro; IPR033298; Cavin2.
DR InterPro; IPR026752; Cavin_fam.
DR PANTHER; PTHR15240; PTHR15240; 1.
DR PANTHER; PTHR15240:SF1; PTHR15240:SF1; 1.
DR Pfam; PF15237; PTRF_SDPR; 1.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; Cytoplasm; Direct protein sequencing;
KW Lipid-binding; Membrane; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.4"
FT CHAIN 2..425
FT /note="Caveolae-associated protein 2"
FT /id="PRO_0000238918"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..168
FT /note="Interaction with CAVIN1"
FT /evidence="ECO:0000250|UniProtKB:Q63918"
FT REGION 62..100
FT /note="Leucine-zipper"
FT /evidence="ECO:0000269|PubMed:19262564"
FT REGION 199..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 271..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 61..82
FT /evidence="ECO:0000255"
FT COILED 125..154
FT /evidence="ECO:0000255"
FT COILED 210..268
FT /evidence="ECO:0000255"
FT COMPBIAS 220..234
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..317
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylglycine"
FT /evidence="ECO:0000269|Ref.4"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63918"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63918"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q66H98"
FT MOD_RES 196
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 199
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 218
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 283
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63918"
FT MOD_RES 284
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63918"
FT MOD_RES 287
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 288
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 293
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19367720, ECO:0007744|PubMed:23186163"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63918"
FT MOD_RES 341
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63918"
FT MOD_RES 366
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63918"
FT MOD_RES 370
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63918"
FT MOD_RES 375
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q63918"
FT MOD_RES 395
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q63918"
FT MOD_RES 403
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q66H98"
FT VARIANT 130
FT /note="E -> D (in dbSNP:rs35012125)"
FT /id="VAR_034422"
FT MUTAGEN 86
FT /note="L->E: Loss of localization in caveolae; when
FT associated with E-93 or E-100."
FT /evidence="ECO:0000269|PubMed:19262564"
FT MUTAGEN 93
FT /note="I->E: Loss of localization in caveolae; when
FT associated with E-86 or E-100."
FT /evidence="ECO:0000269|PubMed:19262564"
FT MUTAGEN 100
FT /note="L->E: Loss of localization in caveolae; when
FT associated with E-86 or E-93."
FT /evidence="ECO:0000269|PubMed:19262564"
SQ SEQUENCE 425 AA; 47173 MW; 0631CBF4BED537F9 CRC64;
MGEDAAQAEK FQHPGSDMRQ EKPSSPSPMP SSTPSPSLNL GNTEEAIRDN SQVNAVTVLT
LLDKLVNMLD AVQENQHKME QRQISLEGSV KGIQNDLTKL SKYQASTSNT VSKLLEKSRK
VSAHTRAVKE RMDRQCAQVK RLENNHAQLL RRNHFKVLIF QEENEIPASV FVKQPVSGAV
EGKEELPDEN KSLEETLHTV DLSSDDDLPH DEEALEDSAE EKVEESRAEK IKRSSLKKVD
SLKKAFSRQN IEKKMNKLGT KIVSVERREK IKKSLTSNHQ KISSGKSSPF KVSPLTFGRK
KVREGESHAE NETKSEDLPS SEQMPNDQEE ESFAEGHSEA SLASALVEGE IAEEAAEKAT
SRGSNSGMDS NIDLTIVEDE EEESVALEQA QKVRYEGSYA LTSEEAERSD GDPVQPAVLQ
VHQTS
