ERC2_RAT
ID ERC2_RAT Reviewed; 957 AA.
AC Q8K3M6; Q8CIZ0;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=ERC protein 2;
DE AltName: Full=CAZ-associated structural protein 1;
DE Short=CAST1;
DE Short=Cast;
DE AltName: Full=Cytomatrix protein p110;
GN Name=Erc2; Synonyms=Cast1, Cmbp;
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] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, INTERACTION WITH RIMS1 AND BSN, AND
RP IDENTIFICATION IN A COMPLEX WITH RIMS1 AND UNC13A.
RC STRAIN=Sprague-Dawley;
RX PubMed=12163476; DOI=10.1083/jcb.200202083;
RA Ohtsuka T., Takao-Rikitsu E., Inoue E., Inoue M., Takeuchi M.,
RA Matsubara K., Deguchi-Tawarada M., Satoh K., Morimoto K., Nakanishi H.,
RA Takai Y.;
RT "Cast: a novel protein of the cytomatrix at the active zone of synapses
RT that forms a ternary complex with RIM1 and Munc13-1.";
RL J. Cell Biol. 158:577-590(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
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 PROTEIN SEQUENCE OF 1-17; 276-281; 332-349; 373-383; 406-420; 447-456;
RP 485-496; 521-528; 547-556; 629-659; 666-674; 729-734; 779-787 AND 856-879,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, and Hippocampus;
RA Lubec G., Chen W.-Q., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
RN [4]
RP INTERACTION WITH ERC1.
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 [5]
RP IDENTIFICATION BY 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).
CC -!- FUNCTION: Thought to be involved in the organization of the cytomatrix
CC at the nerve terminals active zone (CAZ) which regulates
CC neurotransmitter release. Seems to act together with BSN. May recruit
CC liprin-alpha proteins to the CAZ.
CC -!- SUBUNIT: Interacts with BSN, ERC1, PPFIA1, PPFIA2, PPFIA3 and PPFIA4.
CC Interacts through its C-terminus with the PDZ domain of RIMS1. Part of
CC a complex consisting of ERC2, RIMS1 and UNC13A.
CC {ECO:0000269|PubMed:12163476, ECO:0000269|PubMed:14723704}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Synapse. Presynaptic active zone
CC {ECO:0000305|PubMed:12163476}. Cytoplasm, cytoskeleton. Note=Localized
CC to the active zone of presynaptic density. Colocalizes with RIMS1 and
CC BSN in early stages of synapse formation.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8K3M6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8K3M6-2; Sequence=VSP_011472, VSP_011473, VSP_011474;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in brain, including
CC hippocampus, cortex, cerebellum, amygdala and olfactory bulb.
CC {ECO:0000269|PubMed:12163476, ECO:0000269|PubMed:12391317}.
CC -!- DEVELOPMENTAL STAGE: Detected at embryonic day E18 and at later stages.
CC The expression does not significantly change during the developmental
CC stages tested. {ECO:0000269|PubMed:12163476}.
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DR EMBL; AY049038; AAL07517.1; -; mRNA.
DR EMBL; AF541925; AAN39292.1; -; mRNA.
DR RefSeq; NP_740768.1; NM_170787.2.
DR AlphaFoldDB; Q8K3M6; -.
DR SMR; Q8K3M6; -.
DR BioGRID; 251731; 1.
DR CORUM; Q8K3M6; -.
DR STRING; 10116.ENSRNOP00000041403; -.
DR iPTMnet; Q8K3M6; -.
DR PhosphoSitePlus; Q8K3M6; -.
DR PaxDb; Q8K3M6; -.
DR PRIDE; Q8K3M6; -.
DR GeneID; 259269; -.
DR KEGG; rno:259269; -.
DR UCSC; RGD:708372; rat. [Q8K3M6-1]
DR CTD; 26059; -.
DR RGD; 708372; Erc2.
DR eggNOG; KOG4809; Eukaryota.
DR InParanoid; Q8K3M6; -.
DR OrthoDB; 446752at2759; -.
DR PhylomeDB; Q8K3M6; -.
DR TreeFam; TF324969; -.
DR PRO; PR:Q8K3M6; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0048788; C:cytoskeleton of presynaptic active zone; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; NAS:UniProtKB.
DR GO; GO:0098982; C:GABA-ergic synapse; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0005798; C:Golgi-associated vesicle; IDA:UniProtKB.
DR GO; GO:0030426; C:growth cone; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0014069; C:postsynaptic density; IDA:RGD.
DR GO; GO:0048786; C:presynaptic active zone; IDA:UniProtKB.
DR GO; GO:0098831; C:presynaptic active zone cytoplasmic component; IDA:SynGO.
DR GO; GO:0042734; C:presynaptic membrane; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0043195; C:terminal bouton; IDA:RGD.
DR GO; GO:0030165; F:PDZ domain binding; IPI:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0098882; F:structural constituent of presynaptic active zone; 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:0048167; P:regulation of synaptic plasticity; IBA:GO_Central.
DR GO; GO:0007416; P:synapse assembly; NAS:UniProtKB.
DR GO; GO:0050808; P:synapse organization; IEP:RGD.
DR GO; GO:0016082; P:synaptic vesicle priming; ISO:RGD.
DR InterPro; IPR019323; ELKS/CAST.
DR InterPro; IPR030625; ERC2.
DR PANTHER; PTHR18861:SF3; PTHR18861:SF3; 1.
DR Pfam; PF10174; Cast; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Coiled coil; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; Phosphoprotein;
KW Reference proteome; Synapse.
FT CHAIN 1..957
FT /note="ERC protein 2"
FT /id="PRO_0000087004"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 760..957
FT /note="Involved in binding to RIMS1"
FT REGION 918..957
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 140..917
FT /evidence="ECO:0000255"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 922..939
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PH08"
FT MOD_RES 666
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PH08"
FT VAR_SEQ 219
FT /note="Q -> QLLDARRTK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12391317"
FT /id="VSP_011472"
FT VAR_SEQ 492..547
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12391317"
FT /id="VSP_011473"
FT VAR_SEQ 687
FT /note="K -> KQAEQLFNQMYNP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12391317"
FT /id="VSP_011474"
FT CONFLICT 436
FT /note="N -> I (in Ref. 2; AAN39292)"
FT /evidence="ECO:0000305"
FT CONFLICT 791
FT /note="F -> D (in Ref. 2; AAN39292)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 957 AA; 110618 MW; E2757D5A53B8D1CE CRC64;
MYGSARTISN PEGSPSRSPR LPRSPRLGHR RTSSGGGGGT GKTLSMENIQ SLNAAYATSG
PMYLSDHEGV ASTTYPKGTM TLGRATNRAV YGGRVTAMGS SPNIASAGLS HTDVLSYTDQ
HGGLGGSSHH HHHQVPSMLR QVRDSTMLDL QAQLKELQRE NDLLRKELDI KDSKLGSSMN
SIKTFWSPEL KKERVLRKEE AARMSVLKEQ MRVSHEENQH LQLTIQALQD ELRTQRDLNH
LLQQESGNRG AEHFTIELTE ENFRRLQAEH DRQAKELFLL RKTLEEMELR IETQKQTLNA
RDESIKKLLE MLQSKGLPSK SLEDDNERTR RMAEAESQVS HLEVILDQKE KENIHLREEL
HRRSQLQPEP AKTKALQTVI EMKDTKIASL ERNIRDLEDE IQMLKANGVL NTEDREEEIK
QIEVYKSHSK FMKTKNDQLK QELSKKESEL LALQTKLETL SNQNSDCKQH IEVLKESLTA
KEQRAAILQT EVDALRLRLE EKESFLNKKT KQLQDLTEEK GTLAGEIRDM KDMLEVKERK
INVLQKKIEN LQEQLRDKDK QLTNLKDRVK SLQTDSSNTD TALATLEEAL SEKERIIERL
KEQRERDDRE RLEEIESFRK ENKDLKEKVN ALQAELTEKE SSLIDLKEHA SSLASAGLKR
DSKLKSLEIA IEQKKEECNK LEAQLKKAHN IEDDSRMNPE FADRLKQLDK EASYYRDECG
KAQAEVDRLL EILKEVENEK NDKDKKIAEL ESLTLRHMKD QNKKVANLKH NQQLEKKKNA
QLLEEVRRRE FSMVDNSQHL QIEELMNALE KTRQELDATK ARLASTQQSL AEKEAHLANL
RMERRKQLEE ILEMKQEALL AAISEKDANI ALLELSASKK KKTQEEVMAL KREKDRLVHQ
LKQQTQNRMK LMADNYDDDH HHYHHHHHHH HHRSPGRSQH SNHRPSPDQD DEEGIWA
