EXOC2_RAT
ID EXOC2_RAT Reviewed; 924 AA.
AC O54921;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Exocyst complex component 2;
DE AltName: Full=Exocyst complex component Sec5;
DE Short=rSec5;
GN Name=Exoc2; Synonyms=Sec5, Sec5l1;
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 [MRNA], PARTIAL PROTEIN SEQUENCE, AND IDENTIFICATION IN
RP EXOCYST COMPLEX.
RC TISSUE=Brain;
RX PubMed=9405631; DOI=10.1073/pnas.94.26.14438;
RA Kee Y., Yoo J.-S., Hazuka C.D., Peterson K.E., Hsu S.-C., Scheller R.H.;
RT "Subunit structure of the mammalian exocyst complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:14438-14443(1997).
RN [2]
RP INTERACTION WITH RALA.
RX PubMed=11744922; DOI=10.1038/ncb720;
RA Sugihara K., Asano S., Tanaka K., Iwamatsu A., Okawa K., Ohta Y.;
RT "The exocyst complex binds the small GTPase RalA to mediate filopodia
RT formation.";
RL Nat. Cell Biol. 4:73-78(2002).
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=18756269; DOI=10.1038/emboj.2008.166;
RA Cascone I., Selimoglu R., Ozdemir C., Del Nery E., Yeaman C., White M.,
RA Camonis J.;
RT "Distinct roles of RalA and RalB in the progression of cytokinesis are
RT supported by distinct RalGEFs.";
RL EMBO J. 27:2375-2387(2008).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-432, AND IDENTIFICATION BY
RP 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).
RN [5]
RP 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 X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-99 IN COMPLEX WITH RALA.
RX PubMed=12839989; DOI=10.1093/emboj/cdg329;
RA Fukai S., Matern H.T., Jagath J.R., Scheller R.H., Brunger A.T.;
RT "Structural basis of the interaction between RalA and Sec5, a subunit of
RT the sec6/8 complex.";
RL EMBO J. 22:3267-3278(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:9405631, PubMed:26582389).
CC Interacts with EXOC3L1 (By similarity). Interacts with GNEFR/DELGEF;
CC this interaction occurs only in the presence of magnesium or manganese
CC and is stimulated by dCTP or GTP (By similarity). Interacts with RALA
CC and RALB (PubMed:11744922, PubMed:12839989). Interacts with ARL13B;
CC regulates ARL13B localization to the cilium membrane.
CC {ECO:0000250|UniProtKB:Q96KP1, ECO:0000250|UniProtKB:Q9D4H1,
CC ECO:0000269|PubMed:11744922, ECO:0000269|PubMed:12839989,
CC ECO:0000269|PubMed:26582389, ECO:0000269|PubMed:9405631}.
CC -!- INTERACTION:
CC O54921; P11233: RALA; Xeno; NbExp=2; IntAct=EBI-1036795, EBI-1036803;
CC -!- SUBCELLULAR LOCATION: Midbody, Midbody ring
CC {ECO:0000305|PubMed:18756269}. Note=Recruitment to the midbody does not
CC 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}.
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DR EMBL; AF032666; AAC01578.1; -; mRNA.
DR PIR; T09220; T09220.
DR RefSeq; NP_599241.2; NM_134414.2.
DR PDB; 1UAD; X-ray; 2.10 A; C/D=1-99.
DR PDBsum; 1UAD; -.
DR AlphaFoldDB; O54921; -.
DR SMR; O54921; -.
DR CORUM; O54921; -.
DR IntAct; O54921; 6.
DR STRING; 10116.ENSRNOP00000050367; -.
DR iPTMnet; O54921; -.
DR PhosphoSitePlus; O54921; -.
DR jPOST; O54921; -.
DR PaxDb; O54921; -.
DR PRIDE; O54921; -.
DR GeneID; 171455; -.
DR KEGG; rno:171455; -.
DR UCSC; RGD:619961; rat.
DR CTD; 55770; -.
DR RGD; 619961; Exoc2.
DR eggNOG; KOG2347; Eukaryota.
DR InParanoid; O54921; -.
DR PhylomeDB; O54921; -.
DR Reactome; R-RNO-264876; Insulin processing.
DR Reactome; R-RNO-5620916; VxPx cargo-targeting to cilium.
DR EvolutionaryTrace; O54921; -.
DR PRO; PR:O54921; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0000145; C:exocyst; IDA:RGD.
DR GO; GO:0090543; C:Flemming body; IEA:UniProtKB-SubCell.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:RGD.
DR GO; GO:0031267; F:small GTPase binding; ISO:RGD.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:0006893; P:Golgi to plasma membrane transport; ISO:RGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:2000535; P:regulation of entry of bacterium into host cell; ISO:RGD.
DR GO; GO:0006904; P:vesicle docking involved in exocytosis; ISO:RGD.
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; Direct protein sequencing;
KW Exocytosis; Phosphoprotein; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..924
FT /note="Exocyst complex component 2"
FT /id="PRO_0000118920"
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:0007744|PubMed:22673903"
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..19
FT /evidence="ECO:0007829|PDB:1UAD"
FT STRAND 23..29
FT /evidence="ECO:0007829|PDB:1UAD"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:1UAD"
FT STRAND 38..43
FT /evidence="ECO:0007829|PDB:1UAD"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:1UAD"
FT STRAND 53..56
FT /evidence="ECO:0007829|PDB:1UAD"
FT STRAND 59..63
FT /evidence="ECO:0007829|PDB:1UAD"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:1UAD"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:1UAD"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:1UAD"
FT STRAND 85..88
FT /evidence="ECO:0007829|PDB:1UAD"
SQ SEQUENCE 924 AA; 104031 MW; 1903C0593B113373 CRC64;
MSRSRQPPLV TGISPNEGIP WTKVTIRGEN LGTGPTDLIG LTICGHNCLL TAEWMSASKI
VCRVGQAKND KGDIIVTTKS GGRGTSTVSF KLLKPEKIGI LDQSAVWVDE MNYYDMRTDR
NKGIPPLSLR PANPLGIEIE KCKLPQKNLE VLFHGMSADF TSENFSAAWY LIENHSNTSF
EQLKMAVTNL KRQANKKSEG SLAYVKGGLS TFFEAQDALS AIHQKLEADG TEKVEGSMTQ
KLENVLNRAS NTADTLFQEV LGRKDKADST RNALNVLQRF KFLFNLPLNI KRNIQKGDYD
VVINDYEKAK SLFGKTEVQV FKKYYAEVEA GIEDLRELLL KKLLETPSTL HDQKRYIRYL
SDLHAPGDPA WQCIGAQHKW TLKLMQDCKE GHMKSLKGNP GPHSPMLDLD NDARPSVLGH
LSQTASLKRG SSFQSGRDDT WRYKTPHRVA FVEKLTKLVL SQLPNFWKLW ISYVNGSLFS
ETAEKSGQIE RSKNVRQRQN DFKKMIQEVM HSLVKLIRGA LLPFSLREGD GRQYGGWEVQ
AELSGQWLAH VIQTIRLTYE SLTALEIPND MLQIIQDLIL DLRIHCIMVT LQHTAEEIKR
LAEKEDWIVD NEGLTSLPCQ FEQSIVHSLQ SLKGVVDCKP GEASVFQQPK TQEEVCQLCI
SIMQVFIYCL EQLSTKPDAD IDTTHLSVDV SSPDLFGSIH EDFGLTSEQR LLIVLSNCCY
LERHTFLNIA EHFEKHNFQG IEKITQVSMA SLKELDQRLF ENYIELKADP IVGSLETGIY
AGYFDWKDCL PPAGVRNYLK EALVNIIAVH AEVFTISKEL VPRVLARVIE AVSEELSRLM
QCVSSFSRNG ALQARLEICA LRDTVAIYLT PESRSSFKQA LEALPQLASG ADKKLLEELL
NKFKSSMHLQ LTCFQAASPT VMKT
