ERC2_MOUSE
ID ERC2_MOUSE Reviewed; 957 AA.
AC Q6PH08; Q80U20; Q8CCP1;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=ERC protein 2;
DE AltName: Full=CAZ-associated structural protein 1;
DE Short=CAST1;
GN Name=Erc2; Synonyms=Cast1, D14Ertd171e, Kiaa0378;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC STRAIN=C57BL/6J; TISSUE=Olfactory bulb;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Embryo;
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 [4]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65 AND SER-666, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12163476}. Synapse
CC {ECO:0000269|PubMed:12163476}. Presynaptic active zone
CC {ECO:0000269|PubMed:12163476}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:12163476}. Note=Localized to the active zone of
CC presynaptic density.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q6PH08-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6PH08-2; Sequence=VSP_012306, VSP_011467;
CC Name=3;
CC IsoId=Q6PH08-3; Sequence=VSP_011469, VSP_011470;
CC Name=4;
CC IsoId=Q6PH08-4; Sequence=VSP_011466, VSP_011468, VSP_011471;
CC -!- TISSUE SPECIFICITY: Expressed throughout the central nervous system,
CC including hippocampus, cortex, cerebellum and olfactory bulb.
CC {ECO:0000269|PubMed:12163476}.
CC -!- MISCELLANEOUS: [Isoform 4]: Due to intron retention. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC65547.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK122265; BAC65547.1; ALT_INIT; mRNA.
DR EMBL; AK032385; BAC27848.1; -; mRNA.
DR EMBL; BC056760; AAH56760.1; -; mRNA.
DR CCDS; CCDS26887.1; -. [Q6PH08-3]
DR RefSeq; NP_808482.2; NM_177814.5. [Q6PH08-3]
DR RefSeq; XP_006519013.1; XM_006518950.3. [Q6PH08-2]
DR AlphaFoldDB; Q6PH08; -.
DR SMR; Q6PH08; -.
DR BioGRID; 232032; 16.
DR IntAct; Q6PH08; 5.
DR MINT; Q6PH08; -.
DR STRING; 10090.ENSMUSP00000087773; -.
DR iPTMnet; Q6PH08; -.
DR PhosphoSitePlus; Q6PH08; -.
DR EPD; Q6PH08; -.
DR jPOST; Q6PH08; -.
DR MaxQB; Q6PH08; -.
DR PaxDb; Q6PH08; -.
DR PeptideAtlas; Q6PH08; -.
DR PRIDE; Q6PH08; -.
DR ProteomicsDB; 275764; -. [Q6PH08-1]
DR ProteomicsDB; 275765; -. [Q6PH08-2]
DR ProteomicsDB; 275766; -. [Q6PH08-3]
DR ProteomicsDB; 275767; -. [Q6PH08-4]
DR Antibodypedia; 46273; 62 antibodies from 20 providers.
DR DNASU; 238988; -.
DR Ensembl; ENSMUST00000090302; ENSMUSP00000087773; ENSMUSG00000040640. [Q6PH08-3]
DR Ensembl; ENSMUST00000210924; ENSMUSP00000147744; ENSMUSG00000040640. [Q6PH08-2]
DR Ensembl; ENSMUST00000211145; ENSMUSP00000147886; ENSMUSG00000040640. [Q6PH08-1]
DR GeneID; 238988; -.
DR KEGG; mmu:238988; -.
DR UCSC; uc007sty.1; mouse. [Q6PH08-4]
DR UCSC; uc007sua.1; mouse. [Q6PH08-3]
DR CTD; 26059; -.
DR MGI; MGI:1098749; Erc2.
DR VEuPathDB; HostDB:ENSMUSG00000040640; -.
DR eggNOG; KOG4809; Eukaryota.
DR GeneTree; ENSGT00650000093320; -.
DR HOGENOM; CLU_009304_0_0_1; -.
DR InParanoid; Q6PH08; -.
DR OMA; EEILEMX; -.
DR OrthoDB; 446752at2759; -.
DR PhylomeDB; Q6PH08; -.
DR TreeFam; TF324969; -.
DR BioGRID-ORCS; 238988; 0 hits in 40 CRISPR screens.
DR ChiTaRS; Erc2; mouse.
DR PRO; PR:Q6PH08; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q6PH08; protein.
DR Bgee; ENSMUSG00000040640; Expressed in piriform cortex and 175 other tissues.
DR ExpressionAtlas; Q6PH08; baseline and differential.
DR Genevisible; Q6PH08; MM.
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:0098982; C:GABA-ergic synapse; IDA:SynGO.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005798; C:Golgi-associated vesicle; ISO:MGI.
DR GO; GO:0030426; C:growth cone; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0048786; C:presynaptic active zone; ISO:MGI.
DR GO; GO:0098831; C:presynaptic active zone cytoplasmic component; IDA:SynGO.
DR GO; GO:0042734; C:presynaptic membrane; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0043195; C:terminal bouton; ISO:MGI.
DR GO; GO:0030165; F:PDZ domain binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0098882; F:structural constituent of presynaptic active zone; IDA:SynGO.
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:0016082; P:synaptic vesicle priming; IDA:SynGO.
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; Phosphoprotein; Reference proteome; Synapse.
FT CHAIN 1..957
FT /note="ERC protein 2"
FT /id="PRO_0000087003"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 922..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:0007744|PubMed:21183079"
FT MOD_RES 666
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..325
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_012306"
FT VAR_SEQ 219
FT /note="Q -> QLLDARRTK (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_011466"
FT VAR_SEQ 326..358
FT /note="NERTRRMAEAESQVSHLEVILDQKEKENIHLRE -> MALNRSVQTCFCSKM
FT PCEQQICSH (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_011467"
FT VAR_SEQ 493..515
FT /note="DALRLRLEEKESFLNKKTKQLQD -> RHLLRYWRAGALSHIQCCSWETS
FT (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_011468"
FT VAR_SEQ 516..957
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_011471"
FT VAR_SEQ 752..755
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011469"
FT VAR_SEQ 950..957
FT /note="DDEEGIWA -> LSEGLDKRIAQHCSSILIIYCSLALLTIHQRRPAVAAGLK
FT GRGVFAFTFLLNSVLLD (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011470"
SQ SEQUENCE 957 AA; 110639 MW; 9476977763320323 CRC64;
MYGSARTISN LEGSPSRSPR LPRSPRLGHR RTSSGGGGGT GKTLSMENIQ SLNAAYATSG
PMYLSDHEGV ASTTYPKGTM TLGRATNRAV YGGRVTAMGS SPNIASAGLS HTDVLSYTDQ
HGGLSGSSHH 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 VQMLKANGVL NTEDREEEIK
QIEVYKSHSK FMKTKIDQLK 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 QNKKVANLKY NQQLEKKKNA
QLLEEVRRRE DSMVDNSQHL QIEELMNALE KTRQELDATK ARLASTQQSL AEKEAHLANL
RIERRKQLEE ILEMKQEALL AAISEKDANI ALLELSASKK KKTQEEVMAL KREKDRLVHQ
LKQQTQNRMK LMADNYDEDH HHYHHHHHHH HHRSPGRSQH SNHRPSPDQD DEEGIWA
