ID   VPS50_CHICK             Reviewed;         949 AA.
AC   Q5ZKV9;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Syndetin {ECO:0000250|UniProtKB:Q96JG6};
DE   AltName: Full=Coiled-coil domain-containing protein 132 {ECO:0000305};
DE   AltName: Full=EARP/GARPII complex subunit VPS50 {ECO:0000250|UniProtKB:Q96JG6};
GN   Name=VPS50 {ECO:0000250|UniProtKB:Q96JG6}; Synonyms=CCDC132;
GN   ORFNames=RCJMB04_8p23 {ECO:0000303|PubMed:15642098};
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: Acts as component of the EARP complex that is involved in
CC       endocytic recycling. The EARP complex associates with Rab4-positive
CC       endosomes and promotes recycling of internalized transferrin receptor
CC       (TFRC) to the plasma membrane. {ECO:0000250|UniProtKB:Q96JG6}.
CC   -!- SUBUNIT: Component of the endosome-associated retrograde protein (EARP)
CC       complex. {ECO:0000250|UniProtKB:Q96JG6}.
CC   -!- SUBCELLULAR LOCATION: Recycling endosome
CC       {ECO:0000250|UniProtKB:Q96JG6}. Membrane
CC       {ECO:0000250|UniProtKB:F1LSG8}. Note=Associates with membranes in an
CC       EIPR1-dependent manner. {ECO:0000250|UniProtKB:F1LSG8}.
CC   -!- SIMILARITY: Belongs to the syndetin family. {ECO:0000305}.
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DR   EMBL; AJ719975; CAG31634.1; -; mRNA.
DR   RefSeq; NP_001012872.1; NM_001012854.2.
DR   AlphaFoldDB; Q5ZKV9; -.
DR   SMR; Q5ZKV9; -.
DR   STRING; 9031.ENSGALP00000037320; -.
DR   PaxDb; Q5ZKV9; -.
DR   PRIDE; Q5ZKV9; -.
DR   Ensembl; ENSGALT00000015463; ENSGALP00000015447; ENSGALG00000009500.
DR   GeneID; 420560; -.
DR   KEGG; gga:420560; -.
DR   CTD; 55610; -.
DR   VEuPathDB; HostDB:geneid_420560; -.
DR   eggNOG; KOG2939; Eukaryota.
DR   GeneTree; ENSGT00390000003442; -.
DR   InParanoid; Q5ZKV9; -.
DR   PhylomeDB; Q5ZKV9; -.
DR   PRO; PR:Q5ZKV9; -.
DR   Proteomes; UP000000539; Chromosome 2.
DR   Bgee; ENSGALG00000009500; Expressed in spermatid and 14 other tissues.
DR   ExpressionAtlas; Q5ZKV9; baseline and differential.
DR   GO; GO:1990745; C:EARP complex; ISS:UniProtKB.
DR   GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR   GO; GO:0055037; C:recycling endosome; ISS:UniProtKB.
DR   GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR   GO; GO:0032456; P:endocytic recycling; ISS:UniProtKB.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR019514; Syndetin_C.
DR   InterPro; IPR040047; VPS50.
DR   InterPro; IPR019515; VPS54_N.
DR   PANTHER; PTHR13258; PTHR13258; 1.
DR   Pfam; PF10474; DUF2451; 1.
DR   Pfam; PF10475; Vps54_N; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Endosome; Membrane; Protein transport; Reference proteome;
KW   Transport.
FT   CHAIN           1..949
FT                   /note="Syndetin"
FT                   /id="PRO_0000307267"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          509..581
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          82..104
FT                   /evidence="ECO:0000255"
FT   COILED          198..226
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..22
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        534..561
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   949 AA;  109553 MW;  F6EF8F827FFFF2B5 CRC64;
     MQKIKSLMTR QGLRSPQESV HDLSPIENLR FPTKEELRES WEEPTDPQAQ QEIINSIEEV
     YFSNDAFDIV KYELERLPPV LSLQELEEYR DKLKQQQAAE LERVTSLQNG LQLAAVICAD
     GRRHLNIAKE GFTQTSLGLL ANQRKRQLLI GLLKSLRTIK TLQRTDVRLS EMLEEEDYPG
     AIQLCLECQK AASTFKHYSC ISELNSKLQD TLEQIEEQLD VALSKICKNF DINHYTKVQQ
     AYRLLGKTQT AMDQLHMHFT QAIHNTVFQV VLGYVELCAG NTDTKFQKLQ YKDLCTHITS
     DSYIPCLADL CKALWEVMLS YYRTMQWHEN HDQDEAATVS SVSDGSSVVG TEENSFDRSY
     VKKKLEHGLS RIWQDVQLKV KTYLLGTDLS NFKYDDFIFV LDVISRLMQV GEEFCGSKSE
     VLQESIRKQS VNYFKTYHRT RLEELRMFLE NETWELCPVK SSFDILQLHE FKFMVQSRSP
     SVSPSKQPAS AISTTVTLFE QYCNGGNPFE IQADSKDDET EDVLASNGYE SDEQEKSAYQ
     EYDSDSDVPE ELKRDYVDEQ TGDAPMKSVS RETLRSRKKS DYSLNKGNAP ILTNTTLNVV
     RLVGKYMQMM NILKPIAFDV IHFMSQLFDY YLYAVYTFFG RNDTFESTGL GLSSSRLRTT
     LNRIQESLID LEVSADPTGT LTAAEERKEK VPSPHLSHLV VLTSGSSLYG LAERVVATES
     LVFLAEQFEF LQPHLDAVMP AAKKPFLQQF YSQTVSTANE LRKPVYWIVA AKAIDYEQML
     LLMANVKWDV KEIMSQHNVY VDSLLKEFEE FNRRLNEVSK RVRIPLIVSN ILWEHCMRLA
     NRTLVEGYAN VKKCSNEGRA LMQLDFQQFL MKLEKLTDIR PIPDKEFVET YIKAYYLTEN
     DMERWIKEHR EYSTKHLTNL VNVCLGSHIN KKARQKLLAA IDDIDRPKR