VP26C_MOUSE
ID VP26C_MOUSE Reviewed; 297 AA.
AC O35075; Q542V5;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Vacuolar protein sorting-associated protein 26C {ECO:0000305};
DE AltName: Full=Down syndrome critical region protein 3 homolog;
DE AltName: Full=Down syndrome critical region protein A homolog;
GN Name=Vps26c {ECO:0000312|MGI:MGI:1206040}; Synonyms=Dcra, Dscr3, Dscra;
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 [MRNA].
RX PubMed=9399594; DOI=10.1093/oxfordjournals.jbchem.a021835;
RA Nakamura A., Hattori M., Sakaki Y.;
RT "Isolation of a novel human gene from the Down syndrome critical region of
RT chromosome 21q22.2.";
RL J. Biochem. 122:872-877(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Lung, Spleen, 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: Acts as component of the retriever complex. The retriever
CC complex is a heterotrimeric complex related to retromer cargo-selective
CC complex (CSC) and essential for retromer-independent retrieval and
CC recycling of numerous cargos such as integrin alpha-5/beta-1
CC (ITGA5:ITGB1). The recruitment of the retriever complex to the
CC endosomal membrane involves CCC and WASH complexes. In the endosomes,
CC drives the retriever and recycling of NxxY-motif-containing cargo
CC proteins by coupling to SNX17, a cargo essential for the homeostatic
CC maintenance of numerous cell surface proteins associated with processes
CC that include cell migration, cell adhesion, nutrient supply and cell
CC signaling. {ECO:0000250|UniProtKB:O14972}.
CC -!- SUBUNIT: Component of the heterotrimeric retriever complex formed by
CC VPS26C, VPS29 and VPS35L. Interacts with SNX17; the interaction is
CC direct and associates SNX17 with the retriever complex. Interacts with
CC SNX31; the interaction is direct. {ECO:0000250|UniProtKB:O14972}.
CC -!- SUBCELLULAR LOCATION: Endosome {ECO:0000250|UniProtKB:O14972}.
CC -!- SIMILARITY: Belongs to the VPS26 family. {ECO:0000305}.
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DR EMBL; AB001990; BAA23270.1; -; mRNA.
DR EMBL; AK077485; BAC36824.1; -; mRNA.
DR EMBL; AK077628; BAC36911.1; -; mRNA.
DR EMBL; BC003740; AAH03740.1; -; mRNA.
DR CCDS; CCDS28349.1; -.
DR PIR; JC5699; JC5699.
DR RefSeq; NP_031860.1; NM_007834.3.
DR AlphaFoldDB; O35075; -.
DR SMR; O35075; -.
DR IntAct; O35075; 1.
DR MINT; O35075; -.
DR STRING; 10090.ENSMUSP00000023615; -.
DR iPTMnet; O35075; -.
DR PhosphoSitePlus; O35075; -.
DR EPD; O35075; -.
DR MaxQB; O35075; -.
DR PaxDb; O35075; -.
DR PeptideAtlas; O35075; -.
DR PRIDE; O35075; -.
DR ProteomicsDB; 277502; -.
DR Antibodypedia; 8571; 138 antibodies from 22 providers.
DR DNASU; 13185; -.
DR Ensembl; ENSMUST00000023615; ENSMUSP00000023615; ENSMUSG00000022898.
DR GeneID; 13185; -.
DR KEGG; mmu:13185; -.
DR UCSC; uc008abe.2; mouse.
DR CTD; 10311; -.
DR MGI; MGI:1206040; Vps26c.
DR VEuPathDB; HostDB:ENSMUSG00000022898; -.
DR eggNOG; KOG2717; Eukaryota.
DR GeneTree; ENSGT00950000183064; -.
DR HOGENOM; CLU_056829_0_0_1; -.
DR InParanoid; O35075; -.
DR OMA; RCDIKRS; -.
DR OrthoDB; 1476901at2759; -.
DR PhylomeDB; O35075; -.
DR TreeFam; TF323199; -.
DR BioGRID-ORCS; 13185; 4 hits in 71 CRISPR screens.
DR PRO; PR:O35075; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; O35075; protein.
DR Bgee; ENSMUSG00000022898; Expressed in facial nucleus and 267 other tissues.
DR ExpressionAtlas; O35075; baseline and differential.
DR Genevisible; O35075; MM.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0032456; P:endocytic recycling; ISS:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR Gene3D; 2.60.40.640; -; 2.
DR InterPro; IPR014752; Arrestin-like_C.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR028934; Vps26-related.
DR PANTHER; PTHR12233; PTHR12233; 1.
DR Pfam; PF03643; Vps26; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 1: Evidence at protein level;
KW Endosome; Reference proteome.
FT CHAIN 1..297
FT /note="Vacuolar protein sorting-associated protein 26C"
FT /id="PRO_0000073017"
SQ SEQUENCE 297 AA; 32970 MW; D43BD41A613AA3E9 CRC64;
MGTTLDIKIK RANKVYHAGE MLSGVVVISS KDSVQHQGVS LTMEGTVNLQ LSAKSVGVFE
AFYNSVKPIQ IINSTIDVLK PGKIPSGKTE VPFEFPLLVK GSKVLYETYH GVFVNIQYTL
RCDMRRSLLA KDLTKTCEFI VHSAPQKGKL TPSPVDFTIT PETLQNVKER ASLPKFFIRG
HLNSTNCAIT QPLTGELVVE HSDAAIRSIE LQLVRVETCG CAEGYARDAT EIQNIQIADG
DICRNLSVPL YMVFPRLFTC PTLETTNFKV EFEVNVVVLL HADHLITENF PLKLCRT
