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Database: UniProt
Entry: A0A0Q3MDV3_AMAAE
LinkDB: A0A0Q3MDV3_AMAAE
Original site: A0A0Q3MDV3_AMAAE 
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}.
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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
//
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