ID   A0A0V0VC55_9BILA        Unreviewed;       339 AA.
AC   A0A0V0VC55;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   08-NOV-2023, entry version 23.
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=T09_8850 {ECO:0000313|EMBL:KRX61103.1};
OS   Trichinella sp. T9.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX61103.1, ECO:0000313|Proteomes:UP000054681};
RN   [1] {ECO:0000313|EMBL:KRX61103.1, ECO:0000313|Proteomes:UP000054681}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS409 {ECO:0000313|EMBL:KRX61103.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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:KRX61103.1}.
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DR   EMBL; JYDN01000051; KRX61103.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0VC55; -.
DR   STRING; 181606.A0A0V0VC55; -.
DR   Proteomes; UP000054681; 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:0008168; F:methyltransferase activity; 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; 3.30.1330.30; -; 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; IPR029064; Ribosomal_eL30-like_sf.
DR   InterPro; IPR013123; SpoU_subst-bd.
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   Pfam; PF08032; SpoU_sub_bind; 1.
DR   SUPFAM; SSF55315; L30e-like; 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:UP000054681};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU362040}.
FT   DOMAIN          75..154
FT                   /note="RNA 2-O ribose methyltransferase substrate binding"
FT                   /evidence="ECO:0000259|Pfam:PF08032"
FT   DOMAIN          160..314
FT                   /note="Calcineurin-like phosphoesterase"
FT                   /evidence="ECO:0000259|Pfam:PF12850"
SQ   SEQUENCE   339 AA;  38806 MW;  A645BF8898ACF95B CRC64;
     MLMQQLTRNM SYRARMRLFN KQHPVWFVKC MRRIKKLKPE TFFEEYLGMK YSDPRSYSEF
     KKKLSNLQFI EGQAVCGIQN VKRILLSDSI QVNQLYLALK CNSEQNPNEA AINELIALAK
     RQLIEIHVLS SGMITKISGS ADHEGVCADV TMLPARDGLV LVLGDAHIPH RCAALPKQFR
     RMLLPNKIQH ILCTGNLCTK EQFDFLKSLA SDVHVVKGDF DEDSDNQETK VVTVGQFRIG
     LCHGHQLVPW GDFQVIEMLR RKLNVDIMIT GNTHKLETYE REGIYYINPG SITGAFTPLE
     PNVTPSFVLL DVQQAIVTIY IYKLINDEVK VEKTQYKKT
//