CCD91_MOUSE
ID CCD91_MOUSE Reviewed; 442 AA.
AC Q9D8L5; Q8R3N8; Q9D9E8;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Coiled-coil domain-containing protein 91;
DE AltName: Full=GGA-binding partner;
GN Name=Ccdc91; Synonyms=Ggabp;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Pancreas, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, and Czech II; TISSUE=Brain, and Mammary tumor;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Lung, Pancreas, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9D8L5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9D8L5-2; Sequence=VSP_013245, VSP_013246, VSP_013247;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH24946.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK007017; BAB24830.1; -; mRNA.
DR EMBL; AK007917; BAB25348.2; -; mRNA.
DR EMBL; BC024946; AAH24946.1; ALT_INIT; mRNA.
DR EMBL; BC049073; AAH49073.1; -; mRNA.
DR CCDS; CCDS20707.1; -. [Q9D8L5-1]
DR RefSeq; NP_080187.2; NM_025911.2. [Q9D8L5-1]
DR RefSeq; XP_006507139.1; XM_006507076.1. [Q9D8L5-1]
DR RefSeq; XP_017177203.1; XM_017321714.1.
DR AlphaFoldDB; Q9D8L5; -.
DR SMR; Q9D8L5; -.
DR BioGRID; 211877; 5.
DR MINT; Q9D8L5; -.
DR STRING; 10090.ENSMUSP00000032441; -.
DR iPTMnet; Q9D8L5; -.
DR PhosphoSitePlus; Q9D8L5; -.
DR EPD; Q9D8L5; -.
DR MaxQB; Q9D8L5; -.
DR PaxDb; Q9D8L5; -.
DR PeptideAtlas; Q9D8L5; -.
DR PRIDE; Q9D8L5; -.
DR ProteomicsDB; 265603; -. [Q9D8L5-1]
DR ProteomicsDB; 265604; -. [Q9D8L5-2]
DR Antibodypedia; 24462; 113 antibodies from 18 providers.
DR DNASU; 67015; -.
DR Ensembl; ENSMUST00000032441; ENSMUSP00000032441; ENSMUSG00000030301. [Q9D8L5-1]
DR GeneID; 67015; -.
DR KEGG; mmu:67015; -.
DR UCSC; uc009esy.1; mouse. [Q9D8L5-1]
DR UCSC; uc009esz.1; mouse. [Q9D8L5-2]
DR CTD; 55297; -.
DR MGI; MGI:1914265; Ccdc91.
DR VEuPathDB; HostDB:ENSMUSG00000030301; -.
DR eggNOG; ENOG502QW5U; Eukaryota.
DR GeneTree; ENSGT00390000015899; -.
DR HOGENOM; CLU_050535_1_0_1; -.
DR InParanoid; Q9D8L5; -.
DR OMA; QAHRCEE; -.
DR OrthoDB; 780637at2759; -.
DR PhylomeDB; Q9D8L5; -.
DR TreeFam; TF336441; -.
DR BioGRID-ORCS; 67015; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Ccdc91; mouse.
DR PRO; PR:Q9D8L5; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9D8L5; protein.
DR Bgee; ENSMUSG00000030301; Expressed in seminiferous tubule of testis and 251 other tissues.
DR ExpressionAtlas; Q9D8L5; baseline and differential.
DR Genevisible; Q9D8L5; MM.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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 Alternative splicing; Coiled coil; Golgi apparatus; Membrane;
KW Phosphoprotein; Protein transport; Reference proteome; Transport.
FT CHAIN 1..442
FT /note="Coiled-coil domain-containing protein 91"
FT /id="PRO_0000087479"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1..16
FT /note="GGA1-binding motif"
FT /evidence="ECO:0000250"
FT REGION 48..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 114..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 211..414
FT /note="Homodimerization"
FT /evidence="ECO:0000250"
FT COILED 130..210
FT /evidence="ECO:0000255"
FT COILED 253..318
FT /evidence="ECO:0000255"
FT COILED 346..408
FT /evidence="ECO:0000255"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AY97"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AY97"
FT VAR_SEQ 1..36
FT /note="MDDDDFGGFEAAETFDGEQGGNQAVSPAVPWATFPA -> MPMWNK (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_013245"
FT VAR_SEQ 194..210
FT /note="EKHKQELEDMRKAGHEA -> VHGHLSHRCRPAPPPRV (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_013246"
FT VAR_SEQ 211..442
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_013247"
FT CONFLICT 386
FT /note="M -> T (in Ref. 2; AAH24946)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 442 AA; 50007 MW; C2E53B315F81B110 CRC64;
MDDDDFGGFE AAETFDGEQG GNQAVSPAVP WATFPAVSGV RLSPASPELI LDHDHSSPST
GHLPPDAVIS SADDTHADSS LMSQTISKAQ IQQSAHTHLN IPLFPLGLTD EPSHGALALE
DEPEGPGVHV SNSQLRQKIS SLETKLKASE EEKQRIKKDV ESLMEKHSVL EKGFLKEKEQ
DAVSFQARYR ELQEKHKQEL EDMRKAGHEA LSIIVDEYKA LLQSSVKQQL DAIEKQYVSA
IEKQAHRCEE LLHAQHQRLL DVLDTEKELL REKIQEALTQ QSQEQKESLE KCLQEEMQRN
KETLESAVKL EKEAMKDVIT KAVGEERENL EKVHAEEREL WKTEHARDQE RVAEAIQAAV
QEQQRMSQEA VKAAIVEEQR RSEKAMEEAV KRTRDELVEY VREQRRLDQV TRQRSLSSLE
LFLSCAQKQL SALIATEPVD IE
