RB6I2_RAT
ID RB6I2_RAT Reviewed; 948 AA.
AC Q811U3; Q8CIY9;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=ELKS/Rab6-interacting/CAST family member 1;
DE Short=ERC-1;
DE AltName: Full=CAZ-associated structural protein 2;
DE Short=CAST2;
DE AltName: Full=Rab6-interacting protein 2;
GN Name=Erc1; Synonyms=Cast2, Elks, Rab6ip2;
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 INTERACTION WITH RIMS1 AND CAST1.
RC STRAIN=Sprague-Dawley;
RX PubMed=14723704; DOI=10.1111/j.1356-9597.2004.00697.x;
RA Deguchi-Tawarada M., Inoue E., Takao-Rikitsu E., Inoue M., Ohtsuka T.,
RA Takai Y.;
RT "CAST2: identification and characterization of a protein structurally
RT related to the presynaptic cytomatrix protein CAST.";
RL Genes Cells 9:15-23(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING, TISSUE SPECIFICITY,
RP SUBCELLULAR LOCATION, INTERACTION WITH RIMS1 AND RIMS2, AND MUTAGENESIS OF
RP 943-GLU--ALA-948.
RX PubMed=12391317; DOI=10.1073/pnas.182532999;
RA Wang Y., Liu X., Biederer T., Suedhof T.C.;
RT "A family of RIM-binding proteins regulated by alternative splicing:
RT Implications for the genesis of synaptic active zones.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14464-14469(2002).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-937, 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 [4]
RP STRUCTURE BY NMR OF 939-948 IN COMPLEX WITH RIMS1, AND INTERACTION WITH
RP RIMS1.
RX PubMed=16095618; DOI=10.1016/j.jmb.2005.07.047;
RA Lu J., Li H., Wang Y., Sudhof T.C., Rizo J.;
RT "Solution structure of the RIM1alpha PDZ domain in complex with an ELKS1b
RT C-terminal peptide.";
RL J. Mol. Biol. 352:455-466(2005).
CC -!- FUNCTION: Regulatory subunit of the IKK complex. Probably recruits
CC IkappaBalpha/NFKBIA to the complex (By similarity). May be involved in
CC the organization of the cytomatrix at the nerve terminals active zone
CC (CAZ) which regulates neurotransmitter release. May be involved in
CC vesicle trafficking at the CAZ. May be involved in Rab-6 regulated
CC endosomes to Golgi transport. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with the GTB-bound forms of RAB6A isoform 1 and
CC isoform 2 and with RAB6B. The interaction was strongest with RAB6B,
CC followed by RAB6A isoform 2 and weakest with RAB6A isoform 1 (By
CC similarity). Part of a complex with CHUK, IKBKB and IKBKG. Interacts
CC with CHUK, IKBKB and IKBKG. The interaction with IKBKG is independent
CC of CHUK and IKBKB. Interacts with NFKBIA (By similarity). Isoform 1
CC interacts through its C-terminus with the PDZ domains of RIMS1 and
CC RIMS2. Interacts with ERC2/CAST1. Interacts with SDCCAG8. {ECO:0000250,
CC ECO:0000250|UniProtKB:Q8IUD2, ECO:0000269|PubMed:12391317,
CC ECO:0000269|PubMed:14723704, ECO:0000269|PubMed:16095618}.
CC -!- INTERACTION:
CC Q811U3; Q9JIR4: Rims1; NbExp=8; IntAct=EBI-3507502, EBI-3507436;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250|UniProtKB:Q8IUD2}. Cytoplasm
CC {ECO:0000269|PubMed:12391317}. Membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}. Golgi apparatus membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}. Presynaptic active zone
CC {ECO:0000269|PubMed:12391317}. Note=Recruited on Golgi membranes by
CC RAB6A in a GTP-dependent manner. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=Additional isoforms seem to exist.;
CC Name=1; Synonyms=CAST2a, ERC1b;
CC IsoId=Q811U3-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Isoform 1 is specifically expressed in brain. A
CC further probable isoform is widely expressed outside of brain It is
CC referred to as ERC1a by PubMed:12391317 and characterized by a C-
CC terminus identical to that of isoforms 1 in human and mouse.
CC {ECO:0000269|PubMed:12391317}.
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DR EMBL; AY174115; AAO25554.1; -; mRNA.
DR EMBL; AF541926; AAN39293.1; -; mRNA.
DR RefSeq; NP_740769.2; NM_170788.2. [Q811U3-1]
DR PDB; 1ZUB; NMR; -; B=939-948.
DR PDBsum; 1ZUB; -.
DR AlphaFoldDB; Q811U3; -.
DR SMR; Q811U3; -.
DR BioGRID; 251829; 1.
DR ELM; Q811U3; -.
DR IntAct; Q811U3; 3.
DR MINT; Q811U3; -.
DR STRING; 10116.ENSRNOP00000012397; -.
DR iPTMnet; Q811U3; -.
DR PhosphoSitePlus; Q811U3; -.
DR PaxDb; Q811U3; -.
DR PRIDE; Q811U3; -.
DR GeneID; 266806; -.
DR KEGG; rno:266806; -.
DR UCSC; RGD:628733; rat. [Q811U3-1]
DR CTD; 23085; -.
DR RGD; 628733; Erc1.
DR eggNOG; KOG4809; Eukaryota.
DR InParanoid; Q811U3; -.
DR EvolutionaryTrace; Q811U3; -.
DR PRO; PR:Q811U3; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005813; C:centrosome; ISO:RGD.
DR GO; GO:0036064; C:ciliary basal body; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISS:ParkinsonsUK-UCL.
DR GO; GO:0048788; C:cytoskeleton of presynaptic active zone; IBA:GO_Central.
DR GO; GO:0098982; C:GABA-ergic synapse; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008385; C:IkappaB kinase complex; ISO:RGD.
DR GO; GO:0016020; C:membrane; IDA:ARUK-UCL.
DR GO; GO:0014069; C:postsynaptic density; IDA:ARUK-UCL.
DR GO; GO:0098831; C:presynaptic active zone cytoplasmic component; IDA:SynGO.
DR GO; GO:0045202; C:synapse; ISS:ParkinsonsUK-UCL.
DR GO; GO:0008021; C:synaptic vesicle; IDA:ARUK-UCL.
DR GO; GO:0030165; F:PDZ domain binding; IDA:RGD.
DR GO; GO:0031267; F:small GTPase binding; ISS:ParkinsonsUK-UCL.
DR GO; GO:0098882; F:structural constituent of presynaptic active zone; ISO:RGD.
DR GO; GO:0099635; F:voltage-gated calcium channel activity involved in positive regulation of presynaptic cytosolic calcium levels; ISO:RGD.
DR GO; GO:0007252; P:I-kappaB phosphorylation; ISO:RGD.
DR GO; GO:0048790; P:maintenance of presynaptic active zone structure; IBA:GO_Central.
DR GO; GO:0007274; P:neuromuscular synaptic transmission; IBA:GO_Central.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISO:RGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0048167; P:regulation of synaptic plasticity; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISS:ParkinsonsUK-UCL.
DR GO; GO:0016082; P:synaptic vesicle priming; ISO:RGD.
DR InterPro; IPR019323; ELKS/CAST.
DR Pfam; PF10174; Cast; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell projection;
KW Coiled coil; Cytoplasm; Cytoskeleton; Golgi apparatus; Membrane;
KW Phosphoprotein; Protein transport; Reference proteome; Synapse; Transport.
FT CHAIN 1..948
FT /note="ELKS/Rab6-interacting/CAST family member 1"
FT /id="PRO_0000097178"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 773..801
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 903..948
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 144..920
FT /evidence="ECO:0000255"
FT COMPBIAS 31..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 773..798
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 915..942
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 10
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99MI1"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IUD2"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IUD2"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IUD2"
FT MOD_RES 38
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8IUD2"
FT MOD_RES 55
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99MI1"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IUD2"
FT MOD_RES 94
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IUD2"
FT MOD_RES 796
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99MI1"
FT MOD_RES 937
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MUTAGEN 943
FT /note="E->K,A: No effect on RIMS1 and RIMS2 binding."
FT MUTAGEN 944
FT /note="E->K,A: No effect on RIMS1 and RIMS2 binding."
FT MUTAGEN 945
FT /note="G->D,A: Abolishes RIMS1 and RIMS2 binding."
FT MUTAGEN 946
FT /note="I->D,A: Abolishes RIMS1 and RIMS2 binding."
FT MUTAGEN 947
FT /note="W->D,A: Abolishes RIMS1 and RIMS2 binding."
FT MUTAGEN 948
FT /note="A->D: Abolishes RIMS1 and RIMS2 binding."
FT MUTAGEN 948
FT /note="A->L: Weakens RIMS1 and abolishes RIMS2 binding."
FT CONFLICT 771
FT /note="N -> S (in Ref. 2; AAN39293)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 948 AA; 108818 MW; 7CC15D7B1939561C CRC64;
MYGSARSVGK VEPSSQSPGR SPRLPRSPRL GHRRTNSTGG SSGNSVGGGS GKTLSMENIQ
SLNAAYATSG PMYLSDHENV GAETPKSTMT LGRSGGRLPY GVRMTAMGSS PNIASSGVAS
DTIAFGEHHL PPVSMASTVP HSLRQARDNT IMDLQTQLKE VLRENDLLRK DVEVKESKLS
SSMNSIKTFW SPELKKERAL RKDEASKITI WKEQYRVVQE ENQHMQMTIQ ALQDELRIQR
DLNQLFQQDS SSRTGEPCVA ELTEENFQRL HAEHERQAKE LFLLRKTLEE MELRIETQKQ
TLNARDESIK KLLEMLQSKG LSAKATEEDH ERTRRLAEAE MHVHHLESLL EQKEKENNML
REEMHRRFEN APDSAKTKAL QTVIEMKDSK ISSMERGLRD LEEEIQMLKS NGALSTEERE
EEMKQMEVYR SHSKFMKNKI GQVKQELSRK DTELLALQTK LETLTNQFSD SKQHIEVLKE
SLTAKEQRAA ILQTEVDALR LRLEEKETML NKKTKQIQDM AEEKGTQAGE IHDLKDMLDV
KERKVNVLQK KIENLQEQLR DKEKQMSSLK ERVKSLQADT TNTDTALTTL EEALADKERT
IERLKEQRDR DEREKQEEID TYKKDLKDLK EKVSLLQGDL SEKEASLLDL KEHASSLASS
GLKKDSRLKT LEIALEQKKE ECLKMESQLK KAHEATLEAR ASPEMSDRIQ QLEREIARYK
DESSKAQTEV DRLLEILKEV ENEKNDKDKK IAELESLTSR QVKDQNKKVA NLKHKEQVEK
KKSAQMLEEA RRREDSLSDS SQQLQVEELL MAMEKVKQEL ESMKAKLSST QQSLAEKETH
LTNLRAERRK HLEEVLEMKQ EALLAAISEK DANIALLELS SSKKKTQEEV AALKREKDRL
VQQLKQQTQN RMKLMADNYE DDHFRSSRSN QTNHKPSPDQ DEEEGIWA
