EXOC3_RAT
ID EXOC3_RAT Reviewed; 755 AA.
AC Q62825; Q4QQU2;
DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Exocyst complex component 3;
DE AltName: Full=Exocyst complex component Sec6;
DE Short=rSec6;
GN Name=Exoc3; Synonyms=Sec6, Sec6l1;
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], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=7568183; DOI=10.1073/pnas.92.21.9613;
RA Ting A.E., Hazuka C.D., Hsu S.-C., Kirk M.D., Bean A.J., Scheller R.H.;
RT "rSec6 and rSec8, mammalian homologs of yeast proteins essential for
RT secretion.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:9613-9617(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 IN EXOCYST COMPLEX, AND TISSUE SPECIFICITY.
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 [4]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH EXOC8.
RX PubMed=12954101; DOI=10.1089/153685903322286575;
RA Wang S., Hsu S.C.;
RT "Immunological characterization of exocyst complex subunits in cell
RT differentiation.";
RL Hybrid. Hybridomics 22:159-164(2003).
RN [5]
RP INTERACTION WITH SLC6A9.
RX PubMed=16181645; DOI=10.1016/j.neuropharm.2005.07.021;
RA Cubelos B., Gimenez C., Zafra F.;
RT "The glycine transporter GLYT1 interacts with Sec3, a component of the
RT exocyst complex.";
RL Neuropharmacology 49:935-944(2005).
RN [6]
RP INTERACTION WITH MYRIP.
RX PubMed=17827149; DOI=10.1074/jbc.m705167200;
RA Goehring A.S., Pedroja B.S., Hinke S.A., Langeberg L.K., Scott J.D.;
RT "MyRIP anchors protein kinase A to the exocyst complex.";
RL J. Biol. Chem. 282:33155-33167(2007).
CC -!- FUNCTION: Component of the exocyst complex involved in the docking of
CC exocytic vesicles with fusion sites on the plasma membrane.
CC -!- SUBUNIT: The exocyst complex is composed of EXOC1, EXOC2, EXOC3, EXOC4,
CC EXOC5, EXOC6, EXOC7 and EXOC8 (PubMed:9405631). Interacts with EXOC3L1
CC (By similarity). Interacts with BIRC6/bruce (By similarity). Interacts
CC with MYRIP (By similarity). Interacts with SLC6A9 (PubMed:16181645).
CC {ECO:0000250|UniProtKB:O60645, ECO:0000250|UniProtKB:Q6KAR6,
CC ECO:0000269|PubMed:16181645, ECO:0000269|PubMed:17827149,
CC ECO:0000269|PubMed:9405631}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12954101}.
CC Cytoplasm, perinuclear region {ECO:0000269|PubMed:12954101}. Cell
CC projection, growth cone {ECO:0000269|PubMed:12954101}. Cell projection,
CC neuron projection {ECO:0000269|PubMed:12954101}. Midbody
CC {ECO:0000250|UniProtKB:O60645}. Golgi apparatus
CC {ECO:0000250|UniProtKB:O60645}. Note=Perinuclear in undifferentiated
CC PC12 cells. Redistributes to growing neurites and growth cones during
CC NGF-induced neuronal differentiation (PubMed:12954101). During mitosis,
CC early recruitment to the midbody requires RALA, but not RALB, and
CC EXOC2. In late stages of cytokinesis, localization to the midbody is
CC RALB-dependent (By similarity). {ECO:0000250|UniProtKB:O60645,
CC ECO:0000269|PubMed:12954101}.
CC -!- TISSUE SPECIFICITY: Widely expressed, with highest levels in kidney,
CC followed by brain (at protein level). {ECO:0000269|PubMed:9405631}.
CC -!- SIMILARITY: Belongs to the SEC6 family. {ECO:0000305}.
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DR EMBL; U32575; AAA85505.1; -; mRNA.
DR EMBL; BC097993; AAH97993.1; -; mRNA.
DR RefSeq; NP_001020135.1; NM_001024964.1.
DR RefSeq; XP_006227829.1; XM_006227767.3.
DR RefSeq; XP_006227830.1; XM_006227768.3.
DR AlphaFoldDB; Q62825; -.
DR SMR; Q62825; -.
DR BioGRID; 251644; 1.
DR CORUM; Q62825; -.
DR DIP; DIP-60432N; -.
DR IntAct; Q62825; 2.
DR STRING; 10116.ENSRNOP00000020251; -.
DR iPTMnet; Q62825; -.
DR PhosphoSitePlus; Q62825; -.
DR jPOST; Q62825; -.
DR PaxDb; Q62825; -.
DR PRIDE; Q62825; -.
DR Ensembl; ENSRNOT00000077740; ENSRNOP00000072705; ENSRNOG00000039776.
DR GeneID; 252881; -.
DR KEGG; rno:252881; -.
DR UCSC; RGD:621790; rat.
DR CTD; 11336; -.
DR RGD; 621790; Exoc3.
DR eggNOG; KOG2286; Eukaryota.
DR GeneTree; ENSGT01030000234613; -.
DR HOGENOM; CLU_016260_1_0_1; -.
DR InParanoid; Q62825; -.
DR OMA; MNIGPKT; -.
DR OrthoDB; 391172at2759; -.
DR PhylomeDB; Q62825; -.
DR TreeFam; TF314979; -.
DR Reactome; R-RNO-264876; Insulin processing.
DR Reactome; R-RNO-5620916; VxPx cargo-targeting to cilium.
DR PRO; PR:Q62825; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000039776; Expressed in skeletal muscle tissue and 19 other tissues.
DR Genevisible; Q62825; RN.
DR GO; GO:0000145; C:exocyst; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042734; C:presynaptic membrane; IDA:SynGO.
DR GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR GO; GO:0051601; P:exocyst localization; IBA:GO_Central.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 1.10.357.70; -; 1.
DR InterPro; IPR010326; EXOC3/Sec6.
DR InterPro; IPR042532; EXOC3/Sec6_C.
DR PANTHER; PTHR21292; PTHR21292; 1.
DR Pfam; PF06046; Sec6; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell projection; Coiled coil; Cytoplasm;
KW Direct protein sequencing; Exocytosis; Golgi apparatus; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..755
FT /note="Exocyst complex component 3"
FT /id="PRO_0000118927"
FT COILED 34..62
FT /evidence="ECO:0000255"
FT COILED 618..649
FT /evidence="ECO:0000255"
FT MOD_RES 38
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O60645"
SQ SEQUENCE 755 AA; 86497 MW; 67A9C71A4C0860F9 CRC64;
MCKDSACFST MKETDLEAVA TAVQRVAGML QRPDQLDKVE QYRRREARKK ASVEARLKAA
IQSQLDGVRT GLSQLHNALN DVKDIQQSLA DVSKDWRQSI NTIESLKDVK DAVVQHSQLA
AAVENLKNIF SVPEIVRETQ DLIEQGALLQ AHRKLMDLEC SRDGLMCEQY RMDSGNKRDM
TLIHGYFGST QGLSDELAKQ LWMVLQRSLV TVRRDPTLLV SVVRIIEREE KIDRRILDRK
KQTGFVPPGR PKNWKEKMFA VLDRTVTTRI EGTQADTRES DKMWLVRHLE IIRKYVLDDL
VIAKNLLVQC FPPHYDIFKN LLSMYHQALS IRMQDLASED LEANEIVSLL TWVLNTYTSA
EMMGNVELAP EVDVNALEPL LSPNVVSELL DTYMSTLTSN IIAWLRKALE TDKKDWSKET
EPEADQDGYY QTTLPAIVFQ MFEQNLQVAA QISEDLKTKV LVLCLQQMNS FLSRYKEEAQ
LYKEEHLRNR QHPHCYVQYM VAIINNCQTF KESIISLKRK YLKPETEESL CQSQPSMDGI
LDAIAKEGCS SLLEEVFLDL EQHLNELMTK KWMLGSNAVD IICVTVEDYF NDFAKIKKPY
KKRMTAEAHR RVVVEYLRAV MQKRISFRSA EERKEGAEKM VREAEQLRFL FRKLASGFGE
DADGHCDTIV AVAEVIKLTD PSLLYLEVST LVSKYPDIRD DHIGALLALR GDASRDMKQT
IMETLEQGPM QASPNYVPIF QEIVVPSLNV AKLLK
