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Database: UniProt
Entry: A0A3L8SD62_CHLGU
LinkDB: A0A3L8SD62_CHLGU
Original site: A0A3L8SD62_CHLGU 
ID   A0A3L8SD62_CHLGU        Unreviewed;       182 AA.
AC   A0A3L8SD62;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   13-SEP-2023, entry version 13.
DE   RecName: Full=Vacuolar protein sorting-associated protein 29 {ECO:0000256|ARBA:ARBA00017767, ECO:0000256|RuleBase:RU362040};
DE   AltName: Full=Vesicle protein sorting 29 {ECO:0000256|ARBA:ARBA00031913, ECO:0000256|RuleBase:RU362040};
GN   ORFNames=DV515_00009335 {ECO:0000313|EMBL:RLV99829.1};
OS   Chloebia gouldiae (Gouldian finch) (Erythrura gouldiae).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Passeridae;
OC   Chloebia.
OX   NCBI_TaxID=44316 {ECO:0000313|EMBL:RLV99829.1, ECO:0000313|Proteomes:UP000276834};
RN   [1] {ECO:0000313|EMBL:RLV99829.1, ECO:0000313|Proteomes:UP000276834}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Red01 {ECO:0000313|EMBL:RLV99829.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:RLV99829.1};
RX   PubMed=30282656;
RA   Toomey M.B., Marques C.I., Andrade P., Araujo P.M., Sabatino S.,
RA   Gazda M.A., Afonso S., Lopes R.J., Corbo J.C., Carneiro M.;
RT   "A non-coding region near Follistatin controls head colour polymorphism in
RT   the Gouldian finch.";
RL   Proc. R. Soc. B 285:0-0(2018).
CC   -!- FUNCTION: Acts as component of the retromer cargo-selective complex
CC       (CSC). The CSC is believed to be the core functional component of
CC       retromer or respective retromer complex variants acting to prevent
CC       missorting of selected transmembrane cargo proteins into the lysosomal
CC       degradation pathway. {ECO:0000256|RuleBase:RU362040}.
CC   -!- SUBCELLULAR LOCATION: Endosome membrane
CC       {ECO:0000256|ARBA:ARBA00004481}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004481}.
CC   -!- SIMILARITY: Belongs to the VPS29 family.
CC       {ECO:0000256|ARBA:ARBA00005945, ECO:0000256|RuleBase:RU362040}.
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:RLV99829.1}.
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DR   EMBL; QUSF01000030; RLV99829.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3L8SD62; -.
DR   STRING; 44316.ENSEGOP00005015443; -.
DR   Proteomes; UP000276834; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:GOC.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030904; C:retromer complex; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0042147; P:retrograde transport, endosome to Golgi; IEA:InterPro.
DR   CDD; cd07394; MPP_Vps29; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   InterPro; IPR024654; Calcineurin-like_PHP_lpxH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR000979; Phosphodiesterase_MJ0936/Vps29.
DR   InterPro; IPR028661; Vps29.
DR   NCBIfam; TIGR00040; yfcE; 1.
DR   PANTHER; PTHR11124:SF12; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 29; 1.
DR   PANTHER; PTHR11124; VACUOLAR SORTING PROTEIN VPS29; 1.
DR   Pfam; PF12850; Metallophos_2; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
PE   3: Inferred from homology;
KW   Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW   ECO:0000256|RuleBase:RU362040};
KW   Reference proteome {ECO:0000313|Proteomes:UP000276834};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU362040}.
FT   DOMAIN          1..156
FT                   /note="Calcineurin-like phosphoesterase"
FT                   /evidence="ECO:0000259|Pfam:PF12850"
SQ   SEQUENCE   182 AA;  20518 MW;  AE8660D44BA79041 CRC64;
     MLVLVLGDLH IPHRCNSLPA KFKKLLVPGK IQHILCTGNL CTKDTYDYLK TLAGDVHVVR
     GDFDENLNYP EQKVVTVGQF KIGLIHGHQV IPWGDMASLA LLQRQFDVDI LISGHTHKFE
     AFEHENKFYI NPGSATGAYH ALENNIIPSF VLMDIQASTV VTYVYQLIGD DVKVERIEYK
     KS
//
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