ID A0A0Q3MDV3_AMAAE Unreviewed; 449 AA.
AC A0A0Q3MDV3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 22-FEB-2023, entry version 28.
DE RecName: Full=Clusterin {ECO:0000256|ARBA:ARBA00020334, ECO:0000256|PIRNR:PIRNR002368};
GN ORFNames=AAES_89555 {ECO:0000313|EMBL:KQK80821.1};
OS Amazona aestiva (Blue-fronted Amazon parrot).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Psittaciformes; Psittacidae; Amazona.
OX NCBI_TaxID=12930 {ECO:0000313|EMBL:KQK80821.1, ECO:0000313|Proteomes:UP000051836};
RN [1] {ECO:0000313|EMBL:KQK80821.1, ECO:0000313|Proteomes:UP000051836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FVVF132 {ECO:0000313|EMBL:KQK80821.1};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Functions as extracellular chaperone that prevents
CC aggregation of non native proteins. Prevents stress-induced aggregation
CC of blood plasma proteins. {ECO:0000256|PIRNR:PIRNR002368}.
CC -!- SUBUNIT: Antiparallel disulfide-linked heterodimer of an alpha chain
CC and a beta chain. Self-associates and forms higher oligomers.
CC {ECO:0000256|PIRNR:PIRNR002368}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|ARBA:ARBA00004514}. Cytoplasmic vesicle, secretory
CC vesicle, chromaffin granule {ECO:0000256|ARBA:ARBA00004248}.
CC Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004240}. Membrane
CC {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004287}. Mitochondrion membrane
CC {ECO:0000256|ARBA:ARBA00004346}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004346}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004346}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}. Secreted
CC {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|PIRNR:PIRNR002368}.
CC -!- SIMILARITY: Belongs to the clusterin family.
CC {ECO:0000256|ARBA:ARBA00010069, ECO:0000256|PIRNR:PIRNR002368,
CC ECO:0000256|RuleBase:RU000629}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQK80821.1}.
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; LMAW01002506; KQK80821.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q3MDV3; -.
DR STRING; 12930.A0A0Q3MDV3; -.
DR Proteomes; UP000051836; Unassembled WGS sequence.
DR GO; GO:0042583; C:chromaffin granule; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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 3: Inferred from homology;
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|PIRNR:PIRNR002368};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000051836};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|PIRNR:PIRNR002368};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|PIRNR:PIRNR002368};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|PIRNR:PIRNR002368"
FT CHAIN 21..449
FT /note="Clusterin"
FT /evidence="ECO:0000256|PIRNR:PIRNR002368"
FT /id="PRO_5005971106"
FT DOMAIN 19..230
FT /note="Clusterin N-terminal"
FT /evidence="ECO:0000259|SMART:SM00030"
FT DOMAIN 231..445
FT /note="Clusterin C-terminal"
FT /evidence="ECO:0000259|SMART:SM00035"
FT COILED 67..97
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 321..366
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 449 AA; 52004 MW; F1B2FFB924D470FC CRC64;
MALLLLPLLS LLLPWGWGQA LVPPSELKQM SAAGSKYIDT EVENAINGVK QMKTLMDKTS
KDHQAILHTL EETKRKKEEA VQLAREKEQQ LAAKQEVCNE TMLALWEECK PCLKHTCMRF
YSRTCHSGSG LVGRQLEEFL NHSSPFSIWV NGERIDSLLE RDQQQERQFE DLEERFGLLE
DGVDDIFQDS TQVYGRMYPF FRAPFGGFRE AFRPPVQHVR FPLRSERLSR ELHPFFQHPH
HGFHRLFQPL LEMTQRMLEE AQGGWEHTLG GFVPESRNSS DDRMVCREIR RNSAGCLRMR
DECEKCREIL SVDCWQTDPA QSQLREQLED ALRLAERFTR RYDDLMRAFQ AEMLNTTSLL
DQLNRQFGWV SRLANLTQGT DGFLQVTTVL SKAPNLEDPS APPDTQVTVQ LFDSEPLSLT
VPGDISWEDP RFMEIVAEQA LRHYKQNAM
//