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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
 
 
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