EXOC2_MOUSE
ID EXOC2_MOUSE Reviewed; 924 AA.
AC Q9D4H1;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Exocyst complex component 2;
DE AltName: Full=Exocyst complex component Sec5;
GN Name=Exoc2; Synonyms=Sec5, Sec5l1;
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; TISSUE=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].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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).
RN [5]
RP INTERACTION WITH ARL13B, AND SUBUNIT.
RX PubMed=26582389; DOI=10.1091/mbc.e15-02-0061;
RA Seixas C., Choi S.Y., Polgar N., Umberger N.L., East M.P., Zuo X.,
RA Moreiras H., Ghossoub R., Benmerah A., Kahn R.A., Fogelgren B., Caspary T.,
RA Lipschutz J.H., Barral D.C.;
RT "Arl13b and the exocyst interact synergistically in ciliogenesis.";
RL Mol. Biol. Cell 27:308-320(2016).
RN [6]
RP STRUCTURE BY NMR OF RALA-BINDING DOMAIN.
RX PubMed=12624092; DOI=10.1074/jbc.m300155200;
RA Mott H.R., Nietlispach D., Hopkins L.J., Mirey G., Camonis J.H., Owen D.;
RT "Structure of the GTPase-binding domain of Sec5 and elucidation of its Ral
RT binding site.";
RL J. Biol. Chem. 278:17053-17059(2003).
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|UniProtKB:Q96KP1}.
CC -!- SUBUNIT: The exocyst complex is composed of EXOC1, EXOC2, EXOC3, EXOC4,
CC EXOC5, EXOC6, EXOC7 and EXOC8 (PubMed:26582389). Interacts with EXOC3L1
CC (PubMed:18480549). Interacts with GNEFR/DELGEF; this interaction occurs
CC only in the presence of magnesium or manganese and is stimulated by
CC dCTP or GTP (By similarity). Interacts with RALA and RALB (By
CC similarity) (PubMed:18480549). Interacts with ARL13B; regulates ARL13B
CC localization to the cilium membrane. {ECO:0000250|UniProtKB:O54921,
CC ECO:0000250|UniProtKB:Q96KP1, ECO:0000269|PubMed:18480549,
CC ECO:0000269|PubMed:26582389}.
CC -!- SUBCELLULAR LOCATION: Midbody, Midbody ring
CC {ECO:0000250|UniProtKB:Q96KP1}. Note=Recruitment to the midbody does
CC not require RALA, nor RALB. Colocalizes with CNTRL/centriolin at the
CC midbody ring. {ECO:0000250|UniProtKB:Q96KP1}.
CC -!- DOMAIN: Interacts with RALA through the TIG domain.
CC -!- SIMILARITY: Belongs to the SEC5 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK016532; BAB30290.1; -; mRNA.
DR EMBL; AK050068; BAC34056.1; -; mRNA.
DR EMBL; BC048154; AAH48154.1; -; mRNA.
DR EMBL; BC049102; AAH49102.1; -; mRNA.
DR CCDS; CCDS26420.1; -.
DR RefSeq; NP_079864.1; NM_025588.2.
DR RefSeq; XP_006516789.1; XM_006516726.2.
DR PDB; 1HK6; NMR; -; A=5-97.
DR PDBsum; 1HK6; -.
DR AlphaFoldDB; Q9D4H1; -.
DR SMR; Q9D4H1; -.
DR BioGRID; 211506; 5.
DR ComplexPortal; CPX-4982; Exocyst, Exoc6 variant.
DR ComplexPortal; CPX-4983; Exocyst, Exoc6b variant.
DR STRING; 10090.ENSMUSP00000100010; -.
DR iPTMnet; Q9D4H1; -.
DR PhosphoSitePlus; Q9D4H1; -.
DR SwissPalm; Q9D4H1; -.
DR EPD; Q9D4H1; -.
DR MaxQB; Q9D4H1; -.
DR PaxDb; Q9D4H1; -.
DR PeptideAtlas; Q9D4H1; -.
DR PRIDE; Q9D4H1; -.
DR ProteomicsDB; 275701; -.
DR Antibodypedia; 24190; 149 antibodies from 27 providers.
DR DNASU; 66482; -.
DR Ensembl; ENSMUST00000021785; ENSMUSP00000021785; ENSMUSG00000021357.
DR Ensembl; ENSMUST00000102946; ENSMUSP00000100010; ENSMUSG00000021357.
DR GeneID; 66482; -.
DR KEGG; mmu:66482; -.
DR UCSC; uc007pzc.1; mouse.
DR CTD; 55770; -.
DR MGI; MGI:1913732; Exoc2.
DR VEuPathDB; HostDB:ENSMUSG00000021357; -.
DR eggNOG; KOG2347; Eukaryota.
DR GeneTree; ENSGT00390000010872; -.
DR HOGENOM; CLU_005811_0_0_1; -.
DR InParanoid; Q9D4H1; -.
DR OMA; LFPDACG; -.
DR OrthoDB; 97000at2759; -.
DR PhylomeDB; Q9D4H1; -.
DR TreeFam; TF105891; -.
DR Reactome; R-MMU-264876; Insulin processing.
DR Reactome; R-MMU-5620916; VxPx cargo-targeting to cilium.
DR BioGRID-ORCS; 66482; 13 hits in 75 CRISPR screens.
DR ChiTaRS; Exoc2; mouse.
DR EvolutionaryTrace; Q9D4H1; -.
DR PRO; PR:Q9D4H1; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q9D4H1; protein.
DR Bgee; ENSMUSG00000021357; Expressed in manus and 235 other tissues.
DR Genevisible; Q9D4H1; MM.
DR GO; GO:0000145; C:exocyst; ISO:MGI.
DR GO; GO:0090543; C:Flemming body; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IDA:MGI.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:0006893; P:Golgi to plasma membrane transport; ISO:MGI.
DR GO; GO:0090148; P:membrane fission; IC:ComplexPortal.
DR GO; GO:0000281; P:mitotic cytokinesis; IC:ComplexPortal.
DR GO; GO:0045921; P:positive regulation of exocytosis; TAS:MGI.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:2000535; P:regulation of entry of bacterium into host cell; ISO:MGI.
DR GO; GO:0006904; P:vesicle docking involved in exocytosis; ISO:MGI.
DR GO; GO:0090522; P:vesicle tethering involved in exocytosis; IC:ComplexPortal.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR029175; EXOC2/Sec5.
DR InterPro; IPR039481; EXOC2/Sec5_N_dom.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR002909; IPT_dom.
DR PANTHER; PTHR13043; PTHR13043; 1.
DR Pfam; PF15469; Sec5; 1.
DR Pfam; PF01833; TIG; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Coiled coil; Exocytosis; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..924
FT /note="Exocyst complex component 2"
FT /id="PRO_0000118919"
FT DOMAIN 8..93
FT /note="IPT/TIG"
FT COILED 240..260
FT /evidence="ECO:0000255"
FT MOD_RES 431
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96KP1"
FT MOD_RES 432
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96KP1"
FT MOD_RES 435
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96KP1"
FT MOD_RES 440
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96KP1"
FT MOD_RES 454
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q96KP1"
FT STRAND 9..14
FT /evidence="ECO:0007829|PDB:1HK6"
FT STRAND 22..29
FT /evidence="ECO:0007829|PDB:1HK6"
FT TURN 35..37
FT /evidence="ECO:0007829|PDB:1HK6"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:1HK6"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:1HK6"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:1HK6"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:1HK6"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:1HK6"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:1HK6"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:1HK6"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:1HK6"
SQ SEQUENCE 924 AA; 103959 MW; 457BAD92EAA3040B CRC64;
MSRSRQPPLV TGISPNEGIP WTKVTIRGEN LGTGPTDLIG LTICGHNCLL TAEWMSASKI
VCRVGQAKND KGDIIVTTKS GGKGTSTVSF KLLKPEKIGI LDQSAVWVDE MNYYDMRTDR
NKGIPPLSLR PANPLGIEIE KCKLPQKNLE VLFHGMSADF TSENFSAAWY LIENHSTTSF
EQLKMAVTNL KRQANKKSEG SLAYVKGGLS TFFEAQDALS AIHQKLEADG TEKVEGSMTQ
KLENVLNRAS NTADTLFQEV LGRKDKADST RNALNVLQRF KFLFNLPLNI KRNIQKGDYD
VVINDYEKAK SLFGKTEVQV FKKYYAEVEA GIEDLRELLL KKLLETPSTL HDQKRYIRYL
SDLHAPGDPA WQCIGAQHKW TLKLMQDCKE GHMKSLKGHP GPHSPMLDLD NDVRPSVLGH
LSQTASLKRG SSFQSGRDDT WRYKTPHRVA FVEKLTKLVL SQLPNFWKLW ISYVNGSLFS
ETAEKSGQSE RSKNVRQRQN DFKKMIQEVM HSLVKLIRGA LLPLSLREGD GRQYGGWEVQ
AELSGQWLAH VIQTIRLTYE SLTALEIPND MLQIIQDLIL DLRIRCIMVT LQHTAEEIKR
LAEKEDWVVD NEGLTSLPCQ FEQSIVHSLQ SLKGVVDCKP GEASVFQQPK TQEEVCQLCI
NIMQVFIYCL EQLSTKPDAD IDTTHLSVDV SSPDLFGSIH EDFSLTSEQR LLIVLSNCCY
LERHTFLNIA EHFEKHNFQG IEKITQVSMA SLKELDQRLF ENYIELKADP IVGSLEPGIY
AGYFDWKDCL PPAGVRNYLK EALVNIIAVH AEVFTISKEL VPRVLARVVE AVSEELSRLM
QCVSSFSRNG ALQARLEICA LRDTVAIYLT SESRSSFKQA LEALPQLASG ADKKSLEELL
NKFKSSMHLQ LTCFQAASPA VMKT
