ID CLUS_RAT Reviewed; 447 AA.
AC P05371;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 2.
DT 27-MAR-2024, entry version 162.
DE RecName: Full=Clusterin {ECO:0000303|PubMed:3415696};
DE AltName: Full=Dimeric acid glycoprotein;
DE Short=DAG;
DE AltName: Full=Sulfated glycoprotein 2 {ECO:0000303|PubMed:3651384};
DE Short=SGP-2 {ECO:0000303|PubMed:3651384};
DE AltName: Full=Testosterone repressed prostate message 2 {ECO:0000303|PubMed:2299741};
DE Short=TRPM-2 {ECO:0000303|PubMed:7680346};
DE Contains:
DE RecName: Full=Clusterin beta chain;
DE Contains:
DE RecName: Full=Clusterin alpha chain;
DE Flags: Precursor;
GN Name=Clu {ECO:0000312|RGD:3907};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 22-45 AND 227-241,
RP PROTEOLYTIC PROCESSING, GLYCOSYLATION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=3651384; DOI=10.1021/bi00386a008;
RA Collard M.W., Griswold M.D.;
RT "Biosynthesis and molecular cloning of sulfated glycoprotein 2 secreted by
RT rat Sertoli cells.";
RL Biochemistry 26:3297-3303(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Prostate;
RX PubMed=2920020; DOI=10.1042/bj2570293;
RA Bettuzzi S., Hiipakka R.A., Gilna P., Liao S.;
RT "Identification of an androgen-repressed mRNA in rat ventral prostate as
RT coding for sulphated glycoprotein 2 by cDNA cloning and sequence
RT analysis.";
RL Biochem. J. 257:293-296(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=Sprague-Dawley;
RX PubMed=7680346; DOI=10.1016/s0021-9258(18)53497-9;
RA Wong P., Pineault J.M., Lakins J., Taillefer D., Leger J., Wang C.,
RA Tenniswood M.;
RT "Genomic organization and expression of the rat TRPM-2 (clusterin) gene, a
RT gene implicated in apoptosis.";
RL J. Biol. Chem. 268:5021-5031(1993).
RN [4]
RP PROTEIN SEQUENCE OF 22-51 AND 227-256, SUBCELLULAR LOCATION, SUBUNIT, AND
RP PROTEOLYTIC PROCESSING.
RX PubMed=3415696; DOI=10.1016/s0006-291x(88)81051-9;
RA Cheng C.Y., Chen C.C., Feng Z., Marshall A., Bardin C.W.;
RT "Rat clusterin isolated from primary Sertoli cell-enriched culture medium
RT is sulfated glycoprotein-2 (SGP-2).";
RL Biochem. Biophys. Res. Commun. 155:398-404(1988).
RN [5]
RP CHARACTERIZATION OF TRPM-2.
RX PubMed=2299741; DOI=10.1016/s0022-5347(17)39975-5;
RA Bandyk M.G., Sawczuk I.S., Olsson C.A., Katz A.E., Buttyan R.;
RT "Characterization of the products of a gene expressed during androgen-
RT programmed cell death and their potential use as a marker of urogenital
RT injury.";
RL J. Urol. 143:407-413(1990).
RN [6]
RP INTERACTION WITH STMN3, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=16038898; DOI=10.1016/j.yexcr.2005.06.012;
RA Kang S.W., Shin Y.J., Shim Y.J., Jeong S.Y., Park I.S., Min B.H.;
RT "Clusterin interacts with SCLIP (SCG10-like protein) and promotes neurite
RT outgrowth of PC12 cells.";
RL Exp. Cell Res. 309:305-315(2005).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Functions as extracellular chaperone that prevents
CC aggregation of non native proteins. Prevents stress-induced aggregation
CC of blood plasma proteins. Inhibits formation of amyloid fibrils by APP,
CC APOC2, B2M, CALCA, CSN3, SNCA and aggregation-prone LYZ variants (in
CC vitro). Does not require ATP. Maintains partially unfolded proteins in
CC a state appropriate for subsequent refolding by other chaperones, such
CC as HSPA8/HSC70. Does not refold proteins by itself. Binding to cell
CC surface receptors triggers internalization of the chaperone-client
CC complex and subsequent lysosomal or proteasomal degradation. When
CC secreted, protects cells against apoptosis and against cytolysis by
CC complement. Intracellular forms interact with ubiquitin and SCF (SKP1-
CC CUL1-F-box protein) E3 ubiquitin-protein ligase complexes and promote
CC the ubiquitination and subsequent proteasomal degradation of target
CC proteins. Promotes proteasomal degradation of COMMD1 and IKBKB.
CC Modulates NF-kappa-B transcriptional activity (By similarity).
CC Following stress, promotes apoptosis (By similarity). Inhibits
CC apoptosis when associated with the mitochondrial membrane by
CC interference with BAX-dependent release of cytochrome c into the
CC cytoplasm. Plays a role in the regulation of cell proliferation. An
CC intracellular form suppresses stress-induced apoptosis by stabilizing
CC mitochondrial membrane integrity through interaction with HSPA5.
CC Secreted form does not affect caspase or BAX-mediated intrinsic
CC apoptosis and TNF-induced NF-kappa-B-activity (By similarity). Secreted
CC form act as an important modulator during neuronal differentiation
CC through interaction with STMN3 (PubMed:16038898). Plays a role in the
CC clearance of immune complexes that arise during cell injury (By
CC similarity). {ECO:0000250|UniProtKB:P10909,
CC ECO:0000250|UniProtKB:Q06890, ECO:0000269|PubMed:16038898}.
CC -!- SUBUNIT: Antiparallel disulfide-linked heterodimer of an alpha chain
CC and a beta chain (PubMed:3415696). Self-associates and forms higher
CC oligomers. Interacts with a broad range of misfolded proteins,
CC including APP, APOC2 and LYZ. Slightly acidic pH promotes interaction
CC with misfolded proteins. Forms high-molecular weight oligomers upon
CC interaction with misfolded proteins. Interacts with APOA1, LRP2, CLUAP1
CC and PON1. Interacts with the complement complex. Interacts (via alpha
CC chain) with XRCC6. Interacts with SYVN1, COMMD1, BTRC, CUL1 and with
CC ubiquitin and SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase
CC complexes. Interacts (via alpha chain) with BAX in stressed cells,
CC where BAX undergoes a conformation change leading to association with
CC the mitochondrial membrane. Does not interact with BAX in unstressed
CC cells. Found in a complex with LTF, CLU, EPPIN and SEMG1. Interacts
CC (immaturely glycosylated pre-secreted form) with HSPA5; this
CC interaction promotes CLU stability and facilitates stress-induced CLU
CC retrotranslocation from the secretory pathway to the mitochondria,
CC thereby reducing stress-induced apoptosis by stabilizing mitochondrial
CC membrane integrity. Interacts with BCL2L1; this interaction releases
CC and activates BAX and promotes cell death. Interacts with TGFBR2 and
CC ACVR1 (By similarity). Interacts (secreted form) with STMN3; this
CC interaction may act as an important modulator during neuronal
CC differentiation (PubMed:16038898). Interacts with VLDLR and LRP8 (By
CC similarity). {ECO:0000250|UniProtKB:P10909,
CC ECO:0000269|PubMed:16038898, ECO:0000269|PubMed:3415696}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:3415696,
CC ECO:0000269|PubMed:3651384}. Nucleus {ECO:0000250|UniProtKB:P10909}.
CC Cytoplasm {ECO:0000250|UniProtKB:P10909}. Mitochondrion membrane
CC {ECO:0000250|UniProtKB:P10909}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P10909}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P10909}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:16038898}. Microsome
CC {ECO:0000250|UniProtKB:P10909}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:P10909}. Mitochondrion
CC {ECO:0000250|UniProtKB:P10909}. Mitochondrion membrane
CC {ECO:0000250|UniProtKB:P10909}. Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:16038898}. Cytoplasmic vesicle, secretory vesicle,
CC chromaffin granule. Note=Can retrotranslocate from the secretory
CC compartments to the cytosol upon cellular stress. Detected in
CC perinuclear foci that may be aggresomes containing misfolded,
CC ubiquitinated proteins. Detected at the mitochondrion membrane upon
CC induction of apoptosis. Under ER stress, a immaturely glycosylated pre-
CC secreted form retrotranslocates from the endoplasmic reticulum (ER)-
CC Golgi network to the cytoplasm to localize in the mitochondria through
CC HSPA5 interaction. ER stress reduces secretion. Under the stress, minor
CC amounts of non-secreted forms accumulate in cytoplasm.
CC {ECO:0000250|UniProtKB:P10909}.
CC -!- TISSUE SPECIFICITY: Detected in Sertoli cells (at protein level).
CC Detected in cultured Sertoli cells, testis, epididymis, liver and
CC brain. {ECO:0000269|PubMed:3651384}.
CC -!- DEVELOPMENTAL STAGE: Expressed by cells undergoing programmed death as
CC a result of the hormonal stimuli or a traumatic insult.
CC -!- PTM: Proteolytically cleaved on its way through the secretory system,
CC probably within the Golgi lumen (PubMed:3415696, PubMed:3651384).
CC Proteolytic cleavage is not necessary for its chaperone activity. All
CC non-secreted forms are not proteolytically cleaved. Chaperone activity
CC of uncleaved forms is dependent on a non-reducing environment (By
CC similarity). {ECO:0000250|UniProtKB:P10909, ECO:0000269|PubMed:3415696,
CC ECO:0000269|PubMed:3651384}.
CC -!- PTM: Polyubiquitinated, leading to proteasomal degradation. Under
CC cellular stress, the intracellular level of cleaved form is reduced due
CC to proteasomal degradation. {ECO:0000250|UniProtKB:P10909}.
CC -!- PTM: Extensively glycosylated with sulfated N-linked carbohydrates
CC (PubMed:3651384). About 30% of the protein mass is comprised of complex
CC N-linked carbohydrate. Endoplasmic reticulum (ER) stress induces
CC changes in glycosylation status and increases level of hypoglycosylated
CC forms. Core carbohydrates are essential for chaperone activity. Non-
CC secreted forms are hypoglycosylated or unglycosylated (By similarity).
CC {ECO:0000250|UniProtKB:P10909, ECO:0000269|PubMed:3651384}.
CC -!- SIMILARITY: Belongs to the clusterin family. {ECO:0000305}.
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DR EMBL; M16975; AAA41273.1; -; mRNA.
DR EMBL; X13231; CAA31618.1; -; mRNA.
DR EMBL; M64723; AAA42298.1; -; mRNA.
DR EMBL; M64733; AAA42299.1; -; Genomic_DNA.
DR PIR; A45890; A27205.
DR RefSeq; NP_444180.2; NM_053021.2.
DR AlphaFoldDB; P05371; -.
DR SMR; P05371; -.
DR BioGRID; 246971; 2.
DR IntAct; P05371; 1.
DR MINT; P05371; -.
DR STRING; 10116.ENSRNOP00000072116; -.
DR CarbonylDB; P05371; -.
DR GlyCosmos; P05371; 6 sites, No reported glycans.
DR GlyGen; P05371; 6 sites.
DR iPTMnet; P05371; -.
DR PhosphoSitePlus; P05371; -.
DR jPOST; P05371; -.
DR PaxDb; 10116-ENSRNOP00000022095; -.
DR DNASU; 24854; -.
DR GeneID; 24854; -.
DR KEGG; rno:24854; -.
DR UCSC; RGD:3907; rat.
DR AGR; RGD:3907; -.
DR CTD; 1191; -.
DR RGD; 3907; Clu.
DR eggNOG; ENOG502RBQP; Eukaryota.
DR InParanoid; P05371; -.
DR PhylomeDB; P05371; -.
DR Reactome; R-RNO-114608; Platelet degranulation.
DR Reactome; R-RNO-166665; Terminal pathway of complement.
DR Reactome; R-RNO-6803157; Antimicrobial peptides.
DR Reactome; R-RNO-977606; Regulation of Complement cascade.
DR PRO; PR:P05371; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016235; C:aggresome; IDA:RGD.
DR GO; GO:0097440; C:apical dendrite; ISS:Alzheimers_University_of_Toronto.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0042583; C:chromaffin granule; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISS:Alzheimers_University_of_Toronto.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:CAFA.
DR GO; GO:0030426; C:growth cone; IDA:RGD.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:RGD.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0097418; C:neurofibrillary tangle; ISS:Alzheimers_University_of_Toronto.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0099020; C:perinuclear endoplasmic reticulum lumen; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0034366; C:spherical high-density lipoprotein particle; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0001540; F:amyloid-beta binding; ISO:RGD.
DR GO; GO:0050750; F:low-density lipoprotein particle receptor binding; ISO:RGD.
DR GO; GO:0051787; F:misfolded protein binding; ISS:UniProtKB.
DR GO; GO:0140597; F:protein carrier chaperone; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:RGD.
DR GO; GO:0005102; F:signaling receptor binding; ISO:RGD.
DR GO; GO:0048156; F:tau protein binding; ISO:RGD.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISS:UniProtKB.
DR GO; GO:0051082; F:unfolded protein binding; ISS:UniProtKB.
DR GO; GO:0000902; P:cell morphogenesis; ISS:Alzheimers_University_of_Toronto.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; IEP:RGD.
DR GO; GO:0032286; P:central nervous system myelin maintenance; ISS:Alzheimers_University_of_Toronto.
DR GO; GO:0051131; P:chaperone-mediated protein complex assembly; ISS:Alzheimers_University_of_Toronto.
DR GO; GO:0061077; P:chaperone-mediated protein folding; ISS:UniProtKB.
DR GO; GO:0031018; P:endocrine pancreas development; IMP:RGD.
DR GO; GO:0044849; P:estrous cycle; IEP:RGD.
DR GO; GO:0002434; P:immune complex clearance; ISS:UniProtKB.
DR GO; GO:0097193; P:intrinsic apoptotic signaling pathway; ISS:UniProtKB.
DR GO; GO:0001774; P:microglial cell activation; ISS:Alzheimers_University_of_Toronto.
DR GO; GO:0061518; P:microglial cell proliferation; ISS:Alzheimers_University_of_Toronto.
DR GO; GO:1905907; P:negative regulation of amyloid fibril formation; ISS:UniProtKB.
DR GO; GO:1902430; P:negative regulation of amyloid-beta formation; ISS:Alzheimers_University_of_Toronto.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD.
DR GO; GO:1902230; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage; ISS:UniProtKB.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IGI:ARUK-UCL.
DR GO; GO:0031333; P:negative regulation of protein-containing complex assembly; ISS:UniProtKB.
DR GO; GO:1903573; P:negative regulation of response to endoplasmic reticulum stress; ISO:RGD.
DR GO; GO:0048812; P:neuron projection morphogenesis; IMP:RGD.
DR GO; GO:1902004; P:positive regulation of amyloid-beta formation; ISS:Alzheimers_University_of_Toronto.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0045597; P:positive regulation of cell differentiation; IMP:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; IGI:ARUK-UCL.
DR GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; ISS:UniProtKB.
DR GO; GO:1902998; P:positive regulation of neurofibrillary tangle assembly; ISS:Alzheimers_University_of_Toronto.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
DR GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; ISS:Alzheimers_University_of_Toronto.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; ISO:RGD.
DR GO; GO:0048260; P:positive regulation of receptor-mediated endocytosis; ISS:UniProtKB.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISS:Alzheimers_University_of_Toronto.
DR GO; GO:2000060; P:positive regulation of ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0017038; P:protein import; ISS:Alzheimers_University_of_Toronto.
DR GO; GO:0050821; P:protein stabilization; IDA:CAFA.
DR GO; GO:0061740; P:protein targeting to lysosome involved in chaperone-mediated autophagy; ISO:RGD.
DR GO; GO:1900221; P:regulation of amyloid-beta clearance; ISS:Alzheimers_University_of_Toronto.
DR GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
DR GO; GO:0042127; P:regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:1902847; P:regulation of neuronal signal transduction; ISS:Alzheimers_University_of_Toronto.
DR GO; GO:0009416; P:response to light stimulus; IEP:RGD.
DR GO; GO:0051788; P:response to misfolded protein; ISS:UniProtKB.
DR GO; GO:0035864; P:response to potassium ion; IEP:RGD.
DR GO; GO:0009615; P:response to virus; ISO:RGD.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR InterPro; IPR016016; Clusterin.
DR InterPro; IPR000753; Clusterin-like.
DR InterPro; IPR016015; Clusterin_C.
DR InterPro; IPR033986; Clusterin_CS.
DR InterPro; IPR016014; Clusterin_N.
DR PANTHER; PTHR10970; CLUSTERIN; 1.
DR PANTHER; PTHR10970:SF1; CLUSTERIN; 1.
DR Pfam; PF01093; Clusterin; 1.
DR PIRSF; PIRSF002368; Clusterin; 1.
DR SMART; SM00035; CLa; 1.
DR SMART; SM00030; CLb; 1.
DR PROSITE; PS00492; CLUSTERIN_1; 1.
DR PROSITE; PS00493; CLUSTERIN_2; 1.
PE 1: Evidence at protein level;
KW Chaperone; Cytoplasm; Cytoplasmic vesicle; Developmental protein;
KW Differentiation; Direct protein sequencing; Disulfide bond;
KW Endoplasmic reticulum; Glycoprotein; Membrane; Microsome; Mitochondrion;
KW Nucleus; Phosphoprotein; Reference proteome; Secreted; Signal;
KW Spermatogenesis; Ubl conjugation.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:3415696,
FT ECO:0000269|PubMed:3651384"
FT CHAIN 22..447
FT /note="Clusterin"
FT /id="PRO_0000005544"
FT CHAIN 22..226
FT /note="Clusterin beta chain"
FT /id="PRO_0000005545"
FT CHAIN 227..447
FT /note="Clusterin alpha chain"
FT /id="PRO_0000005546"
FT MOTIF 77..80
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q06890"
FT MOTIF 441..445
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q06890"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10909"
FT MOD_RES 394
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10909"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:3651384"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:3651384"
FT CARBOHYD 290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:3651384"
FT CARBOHYD 327
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:3651384"
FT CARBOHYD 353
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:3651384"
FT CARBOHYD 373
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:3651384"
FT DISULFID 101..312
FT /note="Interchain (between beta and alpha chains)"
FT /evidence="ECO:0000250"
FT DISULFID 112..304
FT /note="Interchain (between beta and alpha chains)"
FT /evidence="ECO:0000250"
FT DISULFID 115..301
FT /note="Interchain (between beta and alpha chains)"
FT /evidence="ECO:0000250"
FT DISULFID 120..294
FT /note="Interchain (between beta and alpha chains)"
FT /evidence="ECO:0000250"
FT DISULFID 128..284
FT /note="Interchain (between beta and alpha chains)"
FT /evidence="ECO:0000250"
FT CONFLICT 187
FT /note="D -> H (in Ref. 1; AAA41273)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 447 AA; 51375 MW; 9E2FA33E5E0C146E CRC64;
MKILLLCVAL LLTWDNGMVL GEQEFSDNEL QELSTQGSRY VNKEIQNAVQ GVKHIKTLIE
KTNAERKSLL NSLEEAKKKK EGALDDTRDS EMKLKAFPEV CNETMMALWE ECKPCLKHTC
MKFYARVCRS GSGLVGRQLE EFLNQSSPFY FWMNGDRIDS LLESDRQQSQ VLDAMQDSFT
RASGIIDTLF QDRFFTHEPQ DIHHFSPMGF PHKRPHFLYP KSRLVRSLMP LSHYGPLSFH
NMFQPFFDMI HQAQQAMDVQ LHSPALQFPD VDFLKEGEDD PTVCKEIRHN STGCLKMKGQ
CEKCQEILSV DCSTNNPAQA NLRQELNDSL QVAERLTQQY NELLHSLQSK MLNTSSLLEQ
LNDQFTWVSQ LANLTQGDDQ YLRVSTVTTH SSDSEVPSRV TEVVVKLFDS DPITVVLPEE
VSKDNPKFMD TVAEKALQEY RRKSRME
//
