EXOC5_MOUSE
ID EXOC5_MOUSE Reviewed; 708 AA.
AC Q3TPX4; Q80VK3;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Exocyst complex component 5;
DE AltName: Full=Exocyst complex component Sec10;
GN Name=Exoc5; Synonyms=Sec10l1;
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].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Spleen;
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 GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [5]
RP INTERACTION WITH EXOC3L1.
RX PubMed=18480549; DOI=10.2220/biomedres.29.85;
RA Saito T., Shibasaki T., Seino S.;
RT "Involvement of Exoc3l, a protein structurally related to the exocyst
RT subunit Sec6, in insulin secretion.";
RL Biomed. Res. 29:85-91(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-122, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, 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: Component of the exocyst complex involved in the docking of
CC exocytic vesicles with fusion sites on the plasma membrane.
CC {ECO:0000250}.
CC -!- SUBUNIT: The exocyst complex is composed of EXOC1, EXOC2, EXOC3, EXOC4,
CC EXOC5, EXOC6, EXOC7 and EXOC8 (By similarity). Interacts with EXOC3L1
CC (PubMed:18480549). {ECO:0000250|UniProtKB:P97878,
CC ECO:0000269|PubMed:18480549}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O00471}. Midbody
CC {ECO:0000250|UniProtKB:O00471}. Note=Localization at the midbody
CC requires the presence of RALA, EXOC2 and EXOC3.
CC {ECO:0000250|UniProtKB:O00471}.
CC -!- SIMILARITY: Belongs to the SEC10 family. {ECO:0000305}.
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DR EMBL; AK164067; BAE37611.1; -; mRNA.
DR EMBL; AK157473; BAE34093.1; -; mRNA.
DR EMBL; AK167145; BAE39290.1; -; mRNA.
DR EMBL; AK171012; BAE42183.1; -; mRNA.
DR EMBL; CH466605; EDL20783.1; -; Genomic_DNA.
DR EMBL; BC049967; AAH49967.1; -; mRNA.
DR CCDS; CCDS49474.1; -.
DR RefSeq; NP_997097.1; NM_207214.3.
DR AlphaFoldDB; Q3TPX4; -.
DR SMR; Q3TPX4; -.
DR BioGRID; 222868; 2.
DR ComplexPortal; CPX-4982; Exocyst, Exoc6 variant.
DR ComplexPortal; CPX-4983; Exocyst, Exoc6b variant.
DR IntAct; Q3TPX4; 2.
DR MINT; Q3TPX4; -.
DR STRING; 10090.ENSMUSP00000125434; -.
DR iPTMnet; Q3TPX4; -.
DR PhosphoSitePlus; Q3TPX4; -.
DR EPD; Q3TPX4; -.
DR MaxQB; Q3TPX4; -.
DR PaxDb; Q3TPX4; -.
DR PeptideAtlas; Q3TPX4; -.
DR PRIDE; Q3TPX4; -.
DR ProteomicsDB; 275702; -.
DR Antibodypedia; 24095; 127 antibodies from 26 providers.
DR DNASU; 105504; -.
DR Ensembl; ENSMUST00000162175; ENSMUSP00000125434; ENSMUSG00000061244.
DR GeneID; 105504; -.
DR KEGG; mmu:105504; -.
DR UCSC; uc007tjv.2; mouse.
DR CTD; 10640; -.
DR MGI; MGI:2145645; Exoc5.
DR VEuPathDB; HostDB:ENSMUSG00000061244; -.
DR eggNOG; KOG3745; Eukaryota.
DR GeneTree; ENSGT00390000012837; -.
DR HOGENOM; CLU_020771_1_0_1; -.
DR InParanoid; Q3TPX4; -.
DR OMA; PLCKHHY; -.
DR OrthoDB; 225235at2759; -.
DR PhylomeDB; Q3TPX4; -.
DR TreeFam; TF314966; -.
DR Reactome; R-MMU-264876; Insulin processing.
DR Reactome; R-MMU-5620916; VxPx cargo-targeting to cilium.
DR BioGRID-ORCS; 105504; 15 hits in 75 CRISPR screens.
DR ChiTaRS; Exoc5; mouse.
DR PRO; PR:Q3TPX4; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q3TPX4; protein.
DR Bgee; ENSMUSG00000061244; Expressed in manus and 220 other tissues.
DR ExpressionAtlas; Q3TPX4; baseline and differential.
DR Genevisible; Q3TPX4; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0000145; C:exocyst; IBA:GO_Central.
DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:1904019; P:epithelial cell apoptotic process; IMP:MGI.
DR GO; GO:0001736; P:establishment of planar polarity; IMP:MGI.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:0006893; P:Golgi to plasma membrane transport; IBA:GO_Central.
DR GO; GO:0090148; P:membrane fission; IC:ComplexPortal.
DR GO; GO:0000281; P:mitotic cytokinesis; IC:ComplexPortal.
DR GO; GO:1905515; P:non-motile cilium assembly; IMP:MGI.
DR GO; GO:0072659; P:protein localization to plasma membrane; IMP:MGI.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006904; P:vesicle docking involved in exocytosis; IC:ComplexPortal.
DR GO; GO:0090522; P:vesicle tethering involved in exocytosis; IC:ComplexPortal.
DR InterPro; IPR033960; EXOC5/Sec10.
DR InterPro; IPR009976; Sec10-like.
DR PANTHER; PTHR12100; PTHR12100; 1.
DR PANTHER; PTHR12100:SF4; PTHR12100:SF4; 1.
DR Pfam; PF07393; Sec10; 1.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; Cytoplasm; Exocytosis; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O00471"
FT CHAIN 2..708
FT /note="Exocyst complex component 5"
FT /id="PRO_0000118944"
FT COILED 40..101
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:O00471"
FT MOD_RES 122
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 395
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P97878"
FT MOD_RES 405
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P97878"
FT MOD_RES 412
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97878"
FT CONFLICT 628
FT /note="G -> D (in Ref. 1; BAE37611)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 708 AA; 81738 MW; 257374EE3EA58356 CRC64;
MATTAELFEE PFVADEYIER LVWRTPGGGS RGGPEAFDPK RLLEEFVNHI QELQIMDERI
QRKVEKLEQQ CQKEAKEFAK KVQELQKSNQ VAFQHFQELD EHISYVATKV CHLGDQLEGV
NTPRQRAVEA QKLMKYFNEF LDGELKSDVF TNSEKIKEAA DVIQKLHLIA QELPFDRFSE
VKSKIASKYH DLECQLIQEF TSAQRRGEVS RMREVAAVLL HFKGYSHCID VYIKQCQEGA
YLRNDIFEDA AILCQRVNKQ VGDIFSNPEA VLAKLIQSVF EIKLQSFVKD QLEECRKSDA
EQYLKSLYDL YTRTTGLSSK LMEFNLGTDK QTFLSKLIKS IFISYLENYI EVEIGYLKSR
SAMILQRYYD SKNHQKRSIG TGGIQDLKER IRQRTNLPLG PSIDTHGETF LSQEVVVNLL
QETKQAFERC HRLSDPSDLP RNAFRIFTIL VEFLCIEHID YALETGLAGI PSSDSRNANL
YFLDVVQQAN TIFHLFDKQF NDHLMPLISS SPKLSECLQK KKEIIEQMEM KLDTGIDRTL
NCMIGQMKHI LAAEQKKTDF KPEDENNVLI QYTNACVKVC VYVRKQVEKI KNSMDGKNVD
TVLMELGVRF HRLIYEHLQQ YSYSCMGGML AICDVAEYRK CAKDFKIPMV LHLFDTLHAL
CNLLVVAPDN LKQVCSGEQL ANLDKNILHS FVQLRADYRS ARLARHFS
