ID   VPS51_CHICK             Reviewed;         787 AA.
AC   Q5ZJ25;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Vacuolar protein sorting-associated protein 51 homolog;
DE   AltName: Full=Protein fat-free homolog;
GN   Name=VPS51; Synonyms=FFR; ORFNames=RCJMB04_21i2;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
CC   -!- FUNCTION: Involved in retrograde transport from early and late
CC       endosomes to the late Golgi. The GARP complex is required for the
CC       maintenance of protein retrieval from endosomes to the TGN, acid
CC       hydrolase sorting, lysosome function, endosomal cholesterol traffic and
CC       autophagy. Acts as component of the EARP complex that is involved in
CC       endocytic recycling. {ECO:0000250|UniProtKB:Q9UID3}.
CC   -!- SUBUNIT: Component of the Golgi-associated retrograde protein (GARP)
CC       complex Component of the endosome-associated retrograde protein (EARP)
CC       complex. {ECO:0000250|UniProtKB:Q9UID3}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network
CC       {ECO:0000250|UniProtKB:Q9UID3}. Recycling endosome
CC       {ECO:0000250|UniProtKB:Q9UID3}. Note=Localizes to the trans-Golgi
CC       network as part of the GARP complex, while it localizes to recycling
CC       endosomes as part of the EARP complex. {ECO:0000250|UniProtKB:Q9UID3}.
CC   -!- SIMILARITY: Belongs to the VPS51 family. {ECO:0000305}.
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DR   EMBL; AJ720609; CAG32268.1; -; mRNA.
DR   RefSeq; NP_001026343.1; NM_001031172.1.
DR   AlphaFoldDB; Q5ZJ25; -.
DR   STRING; 9031.ENSGALP00000039522; -.
DR   PaxDb; Q5ZJ25; -.
DR   Ensembl; ENSGALT00000040323; ENSGALP00000039522; ENSGALG00000004166.
DR   GeneID; 422984; -.
DR   KEGG; gga:422984; -.
DR   CTD; 738; -.
DR   VEuPathDB; HostDB:geneid_422984; -.
DR   eggNOG; KOG2346; Eukaryota.
DR   GeneTree; ENSGT00390000001738; -.
DR   HOGENOM; CLU_020677_0_0_1; -.
DR   InParanoid; Q5ZJ25; -.
DR   OMA; HTIEPRT; -.
DR   OrthoDB; 1305393at2759; -.
DR   PhylomeDB; Q5ZJ25; -.
DR   PRO; PR:Q5ZJ25; -.
DR   Proteomes; UP000000539; Chromosome 5.
DR   Bgee; ENSGALG00000004166; Expressed in brain and 13 other tissues.
DR   GO; GO:0005829; C:cytosol; IEA:GOC.
DR   GO; GO:1990745; C:EARP complex; ISS:UniProtKB.
DR   GO; GO:0000938; C:GARP complex; ISS:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0055037; C:recycling endosome; ISS:UniProtKB.
DR   GO; GO:0032456; P:endocytic recycling; ISS:UniProtKB.
DR   GO; GO:0007030; P:Golgi organization; IBA:GO_Central.
DR   GO; GO:0048193; P:Golgi vesicle transport; IBA:GO_Central.
DR   GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR   GO; GO:0007041; P:lysosomal transport; IBA:GO_Central.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0042147; P:retrograde transport, endosome to Golgi; IBA:GO_Central.
DR   InterPro; IPR014812; Vps51.
DR   PANTHER; PTHR15954; PTHR15954; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Endosome; Golgi apparatus; Lipid transport; Protein transport;
KW   Reference proteome; Transport.
FT   CHAIN           1..787
FT                   /note="Vacuolar protein sorting-associated protein 51
FT                   homolog"
FT                   /id="PRO_0000358914"
FT   REGION          1..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          111..142
FT                   /evidence="ECO:0000255"
FT   COILED          265..287
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        12..26
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   787 AA;  86059 MW;  268E2D2AB29A5E4E CRC64;
     MAEVEAAGSG TETGGGSESG NATGSGSGWR RPHGPLQRYY GPSAAEAAEA TPDPADINGP
     HFDPEVFLTK VRSECRLGEL LSREATLGRE IRALDSDMQT LLYENYNKFI SATDTIRKMK
     VDFRRMEAEM DDLASNMAAI SASSARVSAA LQDRHRRGAQ LAGVQALLRK LQSLVEVPGR
     LRRWAAPGAD PARALHCYAR ARAVLRHYRH LPSFRAIEDE SHSIMAELAQ RLRARLRDDT
     LDPKELTECV EMLLQLEEPP EELCEEFLSQ AGARLEAELA ALEAELPPSD PSGTASTPPP
     ASDILDFVDR GSSAFVSNLC LLAASYRSLF EGRPGSGDGR LEAFASTLTT RYFELLERRL
     ALERGLGDTS LLVRALDRFH RRLRALLELL PAAGAEAGAA LVARAARERV ARYLRALQTF
     FLGCLGDVRQ ALAAPRPPGK DGPGLPDLLA TLSSSVLGQL KAVLAYVQLF TARDVAFASL
     PYFKGEFCVE AVREGLVVAF VRWLCRTARG FADSPAERGA PAAPPALLLL LARLCLDYEA
     TTISYILTLT DEQFPPEDTG PAVTPGPALC AEARGAAQRL LDHYVQVQGA AVAQMLRKSV
     ETRDWLGTVE PRNVRAVMKR VVEDITAIDV QVGQLFEEGV RRAQSSDSSR RAFSVYSSSR
     APGRYAPSYT PSAPMDTHLL SNIQKLFSER IDIFSPVEFN KVSVLTGIIK ISLKTLLECV
     RLRTLGRFGL QQVQVDGHYL QLYLWRFAAD ERVVQGLLDE VAASAAHRCL DPVPMEHSVV
     ELICERG