ID   CCD91_RAT               Reviewed;         442 AA.
AC   Q6AY97;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Coiled-coil domain-containing protein 91;
DE   AltName: Full=GGA-binding partner;
GN   Name=Ccdc91; Synonyms=Ggabp;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43 AND SER-46, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Involved in the regulation of membrane traffic through the
CC       trans-Golgi network (TGN). Functions in close cooperation with the GGAs
CC       in the sorting of hydrolases to lysosomes.
CC       {ECO:0000250|UniProtKB:Q7Z6B0}.
CC   -!- SUBUNIT: Homodimer. Interacts with GGA1, GGA2 and AP1G1.
CC       {ECO:0000250|UniProtKB:Q7Z6B0}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q7Z6B0};
CC       Peripheral membrane protein {ECO:0000250|UniProtKB:Q7Z6B0}. Golgi
CC       apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q7Z6B0};
CC       Peripheral membrane protein {ECO:0000250|UniProtKB:Q7Z6B0}. Golgi
CC       apparatus, trans-Golgi network {ECO:0000250|UniProtKB:Q7Z6B0}.
CC       Note=Colocalizes with GGA1, GGA2 and GGA3.
CC       {ECO:0000250|UniProtKB:Q7Z6B0}.
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DR   EMBL; BC079135; AAH79135.1; -; mRNA.
DR   RefSeq; NP_001014083.1; NM_001014061.1.
DR   RefSeq; XP_008761678.1; XM_008763456.2.
DR   AlphaFoldDB; Q6AY97; -.
DR   SMR; Q6AY97; -.
DR   STRING; 10116.ENSRNOP00000002527; -.
DR   iPTMnet; Q6AY97; -.
DR   PhosphoSitePlus; Q6AY97; -.
DR   jPOST; Q6AY97; -.
DR   PaxDb; Q6AY97; -.
DR   PRIDE; Q6AY97; -.
DR   Ensembl; ENSRNOT00000002527; ENSRNOP00000002527; ENSRNOG00000001847.
DR   GeneID; 312863; -.
DR   KEGG; rno:312863; -.
DR   UCSC; RGD:1359502; rat.
DR   CTD; 55297; -.
DR   RGD; 1359502; Ccdc91.
DR   eggNOG; ENOG502QW5U; Eukaryota.
DR   GeneTree; ENSGT00390000015899; -.
DR   HOGENOM; CLU_050535_1_0_1; -.
DR   InParanoid; Q6AY97; -.
DR   OMA; QAHRCEE; -.
DR   OrthoDB; 780637at2759; -.
DR   PhylomeDB; Q6AY97; -.
DR   PRO; PR:Q6AY97; -.
DR   Proteomes; UP000002494; Chromosome 4.
DR   Bgee; ENSRNOG00000001847; Expressed in testis and 19 other tissues.
DR   Genevisible; Q6AY97; RN.
DR   GO; GO:0005829; C:cytosol; IEA:GOC.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005802; C:trans-Golgi network; ISS:UniProtKB.
DR   GO; GO:0090160; P:Golgi to lysosome transport; ISS:UniProtKB.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR034592; CCDC91.
DR   PANTHER; PTHR35072; PTHR35072; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Golgi apparatus; Membrane; Phosphoprotein; Protein transport;
KW   Reference proteome; Transport.
FT   CHAIN           1..442
FT                   /note="Coiled-coil domain-containing protein 91"
FT                   /id="PRO_0000087481"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1..16
FT                   /note="GGA1-binding motif"
FT   REGION          48..79
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          211..414
FT                   /note="Homodimerization"
FT                   /evidence="ECO:0000250"
FT   COILED          127..213
FT                   /evidence="ECO:0000255"
FT   COILED          248..409
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        61..79
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         43
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         46
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
SQ   SEQUENCE   442 AA;  50166 MW;  5D13F374C4236699 CRC64;
     MDDDDFGGFE AAETFDGEQG GNQAVSPAVP WATFPAVSGV RLSPASPELI LDHDRSSPSS
     GHLRSDAVIS SPDDTRADSS LVNQTISKVQ LQQSAHTHLN IPLFPLGLTD ESNHGALALE
     DEPEGPGVHV SNSQLRQKIS SLETKLKASE EEKQRIKKDV ESLMEKHSVL EKDFLKEKEQ
     DAVSFQARYR ELQEKHKQEL EDMRKAGHEA LSIIVDEYKA LLQSSVKQQL DAIEKQYVSA
     IEKQAHRCEE LLHAQHQRLL EVLDTEKELL KEKIQEALTQ QSQEQKETLG KCLQEEMQKN
     KETLESAVKL EKEAMKDVIT KAVEEERENL EKVHAEEREM WKTEHARDQE RVAEAIQAAV
     QEQQRMSQEA VKAAIAEEQR RSEKAMEEAV KRTRDELVEY VREQRRLDQV TRQRSLSSLE
     LFLSCAQKQL SALIATEPVD IE