RB6I2_MOUSE
ID RB6I2_MOUSE Reviewed; 1120 AA.
AC Q99MI1; Q80TK7; Q8BPL1; Q8C7Y1; Q99MI2;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=ELKS/Rab6-interacting/CAST family member 1 {ECO:0000305};
DE Short=ERC-1;
DE AltName: Full=CAZ-associated structural protein 2 {ECO:0000303|PubMed:14723704};
DE Short=CAST2 {ECO:0000303|PubMed:14723704};
DE AltName: Full=Rab6-interacting protein 2 {ECO:0000303|PubMed:11929610};
GN Name=Erc1 {ECO:0000312|MGI:MGI:2151013};
GN Synonyms=Cast2 {ECO:0000303|PubMed:14723704}, Kiaa1081,
GN Rab6ip2 {ECO:0000303|PubMed:11929610};
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 [MRNA] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND INTERACTION WITH RAB6A AND RAB6B.
RX PubMed=11929610; DOI=10.1034/j.1600-0854.2002.030406.x;
RA Monier S., Jollivet F., Janoueix-Lerosey I., Johannes L., Goud B.;
RT "Characterization of novel Rab6-interacting proteins involved in endosome-
RT to-TGN transport.";
RL Traffic 3:289-297(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND SUBCELLULAR LOCATION.
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-351 (ISOFORMS 1/2).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Eye;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 691-1120 (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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-55; SER-75 AND
RP SER-824, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-965 (ISOFORM 2), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-10, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
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. Part of a
CC complex with CHUK, IKBKB and IKBKG. Interacts with CHUK, IKBKB and
CC IKBKG. The interaction with IKBKG is independent of CHUK and IKBKB.
CC Interacts with NFKBIA (By similarity). Isoform 2 interacts through its
CC C-terminus with the PDZ domains of RIMS1 and RIMS2. Interacts with
CC ERC2/CAST1 (By similarity). Interacts with SDCCAG8. {ECO:0000250,
CC ECO:0000250|UniProtKB:Q8IUD2}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250|UniProtKB:Q8IUD2}. Cytoplasm. Membrane;
CC Peripheral membrane protein. Golgi apparatus membrane; Peripheral
CC membrane protein. Presynaptic active zone
CC {ECO:0000269|PubMed:14723704}. Note=Recruited on Golgi membranes by
CC RAB6A in a GTP-dependent manner.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=B, beta;
CC IsoId=Q99MI1-1; Sequence=Displayed;
CC Name=2; Synonyms=A;
CC IsoId=Q99MI1-2; Sequence=VSP_011460, VSP_011462, VSP_011463;
CC Name=3;
CC IsoId=Q99MI1-4; Sequence=VSP_011456, VSP_011457, VSP_011458,
CC VSP_011459;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11929610}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC65719.1; Type=Miscellaneous discrepancy; Note=Artifact. Missing internal sequence that does not correspond to an exon-intron boundary.; Evidence={ECO:0000305};
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DR EMBL; AF340028; AAK26381.1; -; mRNA.
DR EMBL; AF340029; AAK26382.1; -; mRNA.
DR EMBL; AY316692; AAP83581.1; -; mRNA.
DR EMBL; AK048990; BAC33505.1; -; mRNA.
DR EMBL; AK053824; BAC35542.1; -; mRNA.
DR EMBL; AK122437; BAC65719.1; ALT_SEQ; Transcribed_RNA.
DR CCDS; CCDS20476.1; -. [Q99MI1-4]
DR CCDS; CCDS39611.1; -. [Q99MI1-1]
DR RefSeq; NP_835186.1; NM_178085.3. [Q99MI1-4]
DR AlphaFoldDB; Q99MI1; -.
DR SMR; Q99MI1; -.
DR BioGRID; 226265; 12.
DR IntAct; Q99MI1; 10.
DR MINT; Q99MI1; -.
DR STRING; 10090.ENSMUSP00000078534; -.
DR iPTMnet; Q99MI1; -.
DR PhosphoSitePlus; Q99MI1; -.
DR EPD; Q99MI1; -.
DR jPOST; Q99MI1; -.
DR MaxQB; Q99MI1; -.
DR PaxDb; Q99MI1; -.
DR PeptideAtlas; Q99MI1; -.
DR PRIDE; Q99MI1; -.
DR ProteomicsDB; 254993; -. [Q99MI1-1]
DR ProteomicsDB; 254994; -. [Q99MI1-2]
DR ProteomicsDB; 254995; -. [Q99MI1-4]
DR Antibodypedia; 10295; 183 antibodies from 33 providers.
DR Ensembl; ENSMUST00000079582; ENSMUSP00000078534; ENSMUSG00000030172. [Q99MI1-4]
DR Ensembl; ENSMUST00000184838; ENSMUSP00000139030; ENSMUSG00000030172. [Q99MI1-2]
DR GeneID; 111173; -.
DR KEGG; mmu:111173; -.
DR UCSC; uc009dmn.1; mouse. [Q99MI1-4]
DR CTD; 23085; -.
DR MGI; MGI:2151013; Erc1.
DR VEuPathDB; HostDB:ENSMUSG00000030172; -.
DR eggNOG; KOG4809; Eukaryota.
DR GeneTree; ENSGT00650000093320; -.
DR HOGENOM; CLU_815229_0_0_1; -.
DR InParanoid; Q99MI1; -.
DR PhylomeDB; Q99MI1; -.
DR BioGRID-ORCS; 111173; 1 hit in 60 CRISPR screens.
DR ChiTaRS; Erc1; mouse.
DR PRO; PR:Q99MI1; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q99MI1; protein.
DR Bgee; ENSMUSG00000030172; Expressed in undifferentiated genital tubercle and 241 other tissues.
DR ExpressionAtlas; Q99MI1; baseline and differential.
DR Genevisible; Q99MI1; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0036064; C:ciliary basal body; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
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:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008385; C:IkappaB kinase complex; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0098831; C:presynaptic active zone cytoplasmic component; ISO:MGI.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0008021; C:synaptic vesicle; ISO:MGI.
DR GO; GO:0030165; F:PDZ domain binding; ISS:ParkinsonsUK-UCL.
DR GO; GO:0031267; F:small GTPase binding; IDA:MGI.
DR GO; GO:0098882; F:structural constituent of presynaptic active zone; IDA:SynGO.
DR GO; GO:0099635; F:voltage-gated calcium channel activity involved in positive regulation of presynaptic cytosolic calcium levels; IDA:SynGO.
DR GO; GO:0007252; P:I-kappaB phosphorylation; ISO:MGI.
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:MGI.
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:MGI.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IDA:MGI.
DR GO; GO:0016082; P:synaptic vesicle priming; IDA:SynGO.
DR InterPro; IPR019323; ELKS/CAST.
DR InterPro; IPR037245; FIP-RBD_C_sf.
DR InterPro; IPR019018; Rab-bd_FIP-RBD.
DR Pfam; PF10174; Cast; 1.
DR Pfam; PF09457; RBD-FIP; 1.
DR SUPFAM; SSF144270; SSF144270; 1.
DR PROSITE; PS51511; FIP_RBD; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell projection; Coiled coil; Cytoplasm;
KW Cytoskeleton; Golgi apparatus; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Synapse; Transport.
FT CHAIN 1..1120
FT /note="ELKS/Rab6-interacting/CAST family member 1"
FT /id="PRO_0000097177"
FT DOMAIN 1050..1112
FT /note="FIP-RBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00844"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 801..840
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 144..992
FT /evidence="ECO:0000255"
FT COILED 1060..1104
FT /evidence="ECO:0000255"
FT COMPBIAS 31..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 10
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IUD2"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
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:0007744|PubMed:21183079"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 94
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IUD2"
FT MOD_RES 824
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1009
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q811U3"
FT MOD_RES 1050
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8IUD2"
FT VAR_SEQ 1..151
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_011456"
FT VAR_SEQ 440..467
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_011457"
FT VAR_SEQ 525..547
FT /note="DALRLRLEEKETMLNKKTKQIQD -> KSFCDLCRIQSIPSFILLYICYV
FT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_011458"
FT VAR_SEQ 548..1120
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_011459"
FT VAR_SEQ 834..877
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11929610,
FT ECO:0000303|PubMed:12693553"
FT /id="VSP_011460"
FT VAR_SEQ 1013..1020
FT /note="IIQPLLEL -> DEEEGIWA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11929610,
FT ECO:0000303|PubMed:12693553"
FT /id="VSP_011462"
FT VAR_SEQ 1021..1120
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11929610,
FT ECO:0000303|PubMed:12693553"
FT /id="VSP_011463"
FT CONFLICT 121
FT /note="D -> G (in Ref. 3; BAC35542)"
FT /evidence="ECO:0000305"
FT CONFLICT 1070
FT /note="Q -> K (in Ref. 4; BAC65719)"
FT /evidence="ECO:0000305"
FT MOD_RES Q99MI1-2:965
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 1120 AA; 128331 MW; A542B526FAEDF9C7 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 NGALSSEERE
EEMKQMEVYR SHSKFMKNKV EQLKEELSSK DAQGEELKKR AAGLQSEIGQ VKQELSRKDT
ELLALQTKLE TLTNQFSDSK QHIEVLKESL TAKEQRAAIL QTEVDALRLR LEEKETMLNK
KTKQIQDMAE EKGTQAGEIH DLKDMLDVKE RKVNVLQKKI ENLQEQLRDK EKQMSSLKER
VKSLQADTTN TDTALTTLEE ALADKERTIE RLKEQRDRDE REKQEEIDTY KKDLKDLREK
VSLLQGDLSE KEASLLDIKE HASSLASSGL KKDSRLKTLE IALEQKKEEC LKMESQLKKA
HEATLEARAS PEMSDRIQQL EREISRYKDE SSKAQTEVDR LLEILKEVEN EKNDKDKKIA
ELESLTSRQV KDQNKKVANL KHKEQVEKKK SAQMLEEARR REDSLSDSSQ QLQDSLRKKD
DRIEELEEAL RESVQITAER EMVLAQEESA RTNAEKQVEE LLMAMEKVKQ ELESMKAKLS
STQQSLAEKE THLTNLRAER RKHLEEVLEM KQEALLAAIS EKDANIALLE LSSSKKKTQE
EVAALKREKD RLVQQLKQQT QNRMKLMADN YEDDHFRSSR SNQTNHKPSP DQIIQPLLEL
DQNRSKLKLY IGHLTALCHD RDPLILRGLT PPASYNADGE QAAWENELQQ MTQEQLQNEL
EKVEGDNAEL QEFANTILQQ IADHCPDILE QVVNALEESS
