VPS29_DICDI
ID VPS29_DICDI Reviewed; 183 AA.
AC Q54IF7;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Vacuolar protein sorting-associated protein 29;
DE EC=3.1.3.3;
GN Name=vps29; ORFNames=DDB_G0288787;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Plays a role in vesicular protein sorting. Component of the
CC membrane-associated retromer complex which is essential in endosome-to-
CC Golgi retrograde transport. The vps29-vps26-vps35 subcomplex may be
CC involved in cargo selection. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-serine = L-serine + phosphate;
CC Xref=Rhea:RHEA:21208, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57524; EC=3.1.3.3;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-D-serine = D-serine + phosphate;
CC Xref=Rhea:RHEA:24873, ChEBI:CHEBI:15377, ChEBI:CHEBI:35247,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58680; EC=3.1.3.3;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC -!- SUBUNIT: Component of a retromer subcomplex consisting of vps29, vps26
CC and vps35. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Endosome
CC membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305};
CC Cytoplasmic side {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the VPS29 family. {ECO:0000305}.
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DR EMBL; AAFI02000125; EAL63015.1; -; Genomic_DNA.
DR RefSeq; XP_636520.1; XM_631428.1.
DR AlphaFoldDB; Q54IF7; -.
DR SMR; Q54IF7; -.
DR STRING; 44689.DDB0234192; -.
DR PaxDb; Q54IF7; -.
DR EnsemblProtists; EAL63015; EAL63015; DDB_G0288787.
DR GeneID; 8626805; -.
DR KEGG; ddi:DDB_G0288787; -.
DR dictyBase; DDB_G0288787; vps29.
DR eggNOG; KOG3325; Eukaryota.
DR HOGENOM; CLU_063749_0_1_1; -.
DR InParanoid; Q54IF7; -.
DR OMA; IVVYVYE; -.
DR PhylomeDB; Q54IF7; -.
DR Reactome; R-DDI-3238698; WNT ligand biogenesis and trafficking.
DR PRO; PR:Q54IF7; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0032009; C:early phagosome; IDA:dictyBase.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
DR GO; GO:0032010; C:phagolysosome; IDA:dictyBase.
DR GO; GO:0030904; C:retromer complex; ISS:dictyBase.
DR GO; GO:0036424; F:L-phosphoserine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISS:dictyBase.
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; IPR020935; PdiEstase_YfcE_CS.
DR InterPro; IPR000979; Phosphodiesterase_MJ0936/Vps29.
DR InterPro; IPR028661; Vps29.
DR PANTHER; PTHR11124; PTHR11124; 1.
DR PANTHER; PTHR11124:SF12; PTHR11124:SF12; 1.
DR Pfam; PF12850; Metallophos_2; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
DR TIGRFAMs; TIGR00040; yfcE; 1.
DR PROSITE; PS01269; UPF0025; 1.
PE 3: Inferred from homology;
KW Endosome; Hydrolase; Membrane; Metal-binding; Protein transport;
KW Reference proteome; Transport; Zinc.
FT CHAIN 1..183
FT /note="Vacuolar protein sorting-associated protein 29"
FT /id="PRO_0000328097"
FT BINDING 8
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 10
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 39
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 39
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 62
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 115
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 117
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
SQ SEQUENCE 183 AA; 20414 MW; FB8A3619B45FCCE0 CRC64;
MFIIAIGDVH VPHRSYGIPP EFKKLLVPEK IQHILCTGNL VSKEIHDYFK VLTSDVHIVR
GDLDENTSYP DTKIVSIGQF KFGLCHGHQI VPWGDRASLA ALQRQLDVDV LISGHTHVLE
VFESNGKLFV NPGSATGAFS NISNDVIPSF VLMDVQSNNI TVYIYKLIDG QVKVEKIDHV
KQQ
