ENTR1_MOUSE
ID ENTR1_MOUSE Reviewed; 432 AA.
AC A2AIW0; A2AIW1; Q3TQC5; Q6P8W2; Q8BIV5; Q8K0I8; Q9D1V2; Q9D4S1; Q9D5W1;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Endosome-associated-trafficking regulator 1 {ECO:0000305};
DE AltName: Full=Serologically defined colon cancer antigen 3 {ECO:0000303|PubMed:16332174};
GN Name=Entr1 {ECO:0000250|UniProtKB:Q96C92}; Synonyms=Sdccag3;
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] (ISOFORMS 2; 3; 4 AND 5).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Hippocampus, and Testis;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 6).
RC STRAIN=FVB/N; TISSUE=Brain, and Kidney;
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 FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16332174; DOI=10.1089/dna.2005.24.777;
RA Neznanov N., Neznanova L., Angres B., Gudkov A.V.;
RT "Serologically defined colon cancer antigen 3 is necessary for the
RT presentation of TNF receptor 1 on cell surface.";
RL DNA Cell Biol. 24:777-785(2005).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241 AND SER-245,
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18 (ISOFORM 3), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, 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 INTERACTION WITH GIT1.
RX PubMed=23108400; DOI=10.1038/onc.2012.485;
RA Hagemann N., Ackermann N., Christmann J., Brier S., Yu F., Erdmann K.S.;
RT "The serologically defined colon cancer antigen-3 interacts with the
RT protein tyrosine phosphatase PTPN13 and is involved in the regulation of
RT cytokinesis.";
RL Oncogene 32:4602-4613(2013).
CC -!- FUNCTION: May be involved in modulation of TNF response. May be
CC involved in presentation of TNFRSF1A on the cell surface
CC (PubMed:16332174). Involved in the endosome-to-plasma membrane
CC trafficking and recycling of SNX27-retromer-dependent cargo proteins,
CC such as GLUT1. Involved in the regulation of cytokinesis; the function
CC may involve PTPN13 and GIT1 (By similarity).
CC {ECO:0000250|UniProtKB:Q96C92, ECO:0000269|PubMed:16332174}.
CC -!- FUNCTION: Endosome-associated protein that plays a role in membrane
CC receptor sorting, cytokinesis and ciliogenesis. Involved in the
CC endosome-to-plasma membrane trafficking and recycling of SNX27-
CC retromer-dependent cargo proteins, such as GLUT1. Involved in the
CC regulation of cytokinesis; the function may involve PTPN13 and GIT1.
CC Plays a role in the formation of cilia. Involved in cargo protein
CC localization, such as PKD2, at primary cilia (By similarity). Involved
CC in the presentation of the tumor necrosis factor (TNF) receptor
CC TNFRSF1A on the cell surface, and hence in the modulation of the TNF-
CC induced apoptosis (PubMed:16332174). {ECO:0000250|UniProtKB:Q96C92,
CC ECO:0000269|PubMed:16332174}.
CC -!- SUBUNIT: Found in a complex with ENTR1, PTPN13 and GIT1. Interacts with
CC PTPN13 (via the FERM domain) (By similarity). Interacts (via N-
CC terminus) with GIT1 (via N- and C-terminus); this interaction is direct
CC (PubMed:23108400). Interacts with NOD2. Interacts (via N-terminus) with
CC IFT88. Interacts with VPS35. {ECO:0000250|UniProtKB:Q96C92,
CC ECO:0000269|PubMed:23108400}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16332174}. Early
CC endosome {ECO:0000250|UniProtKB:Q96C92}. Endosome
CC {ECO:0000250|UniProtKB:Q96C92}. Recycling endosome
CC {ECO:0000250|UniProtKB:Q96C92}. Midbody {ECO:0000250|UniProtKB:Q96C92}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:Q96C92}. Cytoplasm, cytoskeleton, cilium basal
CC body {ECO:0000250|UniProtKB:Q96C92}. Note=Colocalizes in a WASHC2-
CC dependent manner with the retromer CSC complex at endosomes. During
CC cytokinesis colocalized with PTPN13 at the midbody. Colocalizes with
CC IFT88 and gamma-tubulin at the basal body of primary cilia. Colocalizes
CC with IFT88 and pericentrin at the centrosome.
CC {ECO:0000250|UniProtKB:Q96C92}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=A2AIW0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A2AIW0-2; Sequence=VSP_032180;
CC Name=3;
CC IsoId=A2AIW0-3; Sequence=VSP_032179;
CC Name=4;
CC IsoId=A2AIW0-4; Sequence=VSP_032178;
CC Name=5;
CC IsoId=A2AIW0-5; Sequence=VSP_032183;
CC Name=6;
CC IsoId=A2AIW0-6; Sequence=VSP_032180, VSP_032181, VSP_032182;
CC -!- DOMAIN: Tne N-terminal domain is necessary and sufficient for basal
CC body localization and ciliogenesis. {ECO:0000250|UniProtKB:Q96C92}.
CC -!- PTM: Phosphorylated. {ECO:0000250|UniProtKB:Q96C92}.
CC -!- SIMILARITY: Belongs to the ENTR1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB30158.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB32357.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK082787; BAC38620.1; -; mRNA.
DR EMBL; AK016227; BAB30158.1; ALT_INIT; mRNA.
DR EMBL; AK021273; BAB32357.1; ALT_FRAME; mRNA.
DR EMBL; AK014885; BAB29602.1; -; mRNA.
DR EMBL; AK163690; BAE37459.1; -; mRNA.
DR EMBL; AL732541; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC031199; AAH31199.1; -; mRNA.
DR EMBL; BC061037; AAH61037.1; -; mRNA.
DR CCDS; CCDS15803.2; -. [A2AIW0-1]
DR CCDS; CCDS50540.1; -. [A2AIW0-3]
DR CCDS; CCDS50541.1; -. [A2AIW0-2]
DR RefSeq; NP_001078876.1; NM_001085407.1. [A2AIW0-2]
DR RefSeq; NP_001078877.1; NM_001085408.1. [A2AIW0-3]
DR RefSeq; NP_080839.2; NM_026563.3. [A2AIW0-1]
DR AlphaFoldDB; A2AIW0; -.
DR SMR; A2AIW0; -.
DR STRING; 10090.ENSMUSP00000109737; -.
DR iPTMnet; A2AIW0; -.
DR PhosphoSitePlus; A2AIW0; -.
DR jPOST; A2AIW0; -.
DR MaxQB; A2AIW0; -.
DR PaxDb; A2AIW0; -.
DR PRIDE; A2AIW0; -.
DR ProteomicsDB; 256719; -. [A2AIW0-1]
DR ProteomicsDB; 256720; -. [A2AIW0-2]
DR ProteomicsDB; 256721; -. [A2AIW0-3]
DR ProteomicsDB; 256722; -. [A2AIW0-4]
DR ProteomicsDB; 256723; -. [A2AIW0-5]
DR ProteomicsDB; 256724; -. [A2AIW0-6]
DR Antibodypedia; 32151; 149 antibodies from 22 providers.
DR Ensembl; ENSMUST00000028293; ENSMUSP00000028293; ENSMUSG00000026927. [A2AIW0-2]
DR Ensembl; ENSMUST00000077983; ENSMUSP00000077133; ENSMUSG00000026927. [A2AIW0-3]
DR Ensembl; ENSMUST00000114102; ENSMUSP00000109737; ENSMUSG00000026927. [A2AIW0-1]
DR GeneID; 68112; -.
DR KEGG; mmu:68112; -.
DR UCSC; uc008iuy.1; mouse. [A2AIW0-1]
DR UCSC; uc008iuz.1; mouse. [A2AIW0-2]
DR UCSC; uc008iva.1; mouse. [A2AIW0-3]
DR UCSC; uc008ivb.1; mouse. [A2AIW0-5]
DR UCSC; uc008ivc.1; mouse. [A2AIW0-6]
DR CTD; 10807; -.
DR MGI; MGI:1915362; Entr1.
DR VEuPathDB; HostDB:ENSMUSG00000026927; -.
DR eggNOG; ENOG502QUJK; Eukaryota.
DR GeneTree; ENSGT00390000000560; -.
DR InParanoid; A2AIW0; -.
DR OMA; LEYPQPF; -.
DR OrthoDB; 1429935at2759; -.
DR PhylomeDB; A2AIW0; -.
DR TreeFam; TF335840; -.
DR BioGRID-ORCS; 68112; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Sdccag3; mouse.
DR PRO; PR:A2AIW0; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; A2AIW0; protein.
DR Bgee; ENSMUSG00000026927; Expressed in seminiferous tubule of testis and 249 other tissues.
DR ExpressionAtlas; A2AIW0; baseline and differential.
DR Genevisible; A2AIW0; MM.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; ISS:UniProtKB.
DR GO; GO:0005769; C:early endosome; ISO:MGI.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0030496; C:midbody; ISO:MGI.
DR GO; GO:0055037; C:recycling endosome; ISO:MGI.
DR GO; GO:0030904; C:retromer complex; ISO:MGI.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0030030; P:cell projection organization; IEA:UniProtKB-KW.
DR GO; GO:0032456; P:endocytic recycling; ISO:MGI.
DR GO; GO:0045724; P:positive regulation of cilium assembly; ISS:UniProtKB.
DR GO; GO:1903566; P:positive regulation of protein localization to cilium; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0032465; P:regulation of cytokinesis; ISO:MGI.
DR InterPro; IPR026757; ENTR1.
DR PANTHER; PTHR31259; PTHR31259; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Cell projection;
KW Cilium biogenesis/degradation; Coiled coil; Cytoplasm; Cytoskeleton;
KW Endosome; Phosphoprotein; Protein transport; Reference proteome; Transport.
FT CHAIN 1..432
FT /note="Endosome-associated-trafficking regulator 1"
FT /id="PRO_0000324286"
FT REGION 126..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..196
FT /note="Required for interaction with PTPN13"
FT /evidence="ECO:0000250|UniProtKB:Q96C92"
FT REGION 226..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 262..289
FT /evidence="ECO:0000255"
FT COILED 315..370
FT /evidence="ECO:0000255"
FT COMPBIAS 226..242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96C92"
FT MOD_RES 148
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96C92"
FT MOD_RES 241
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 245
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..58
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_032178"
FT VAR_SEQ 24..96
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_032179"
FT VAR_SEQ 24..73
FT /note="Missing (in isoform 2 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_032180"
FT VAR_SEQ 136..143
FT /note="EASRHPLG -> VHLGSCQW (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_032181"
FT VAR_SEQ 144..432
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_032182"
FT VAR_SEQ 272..432
FT /note="LKDENSKLRRKLNEVQSFSETQTEMVRTLERKLEAKMIKEESDFHDLESVVQ
FT QVEQNLELMTKRAVKAENHVLKLKQEINLLQAQLSNLRRENEALRSGQGASLSVVKQNT
FT DVALQNLHLVMNSAHASIKQLVSGADTLNLVAEILKSIDRISEVKDEVDS -> VSEGS
FT VAPNTAELCCGEELQSSTSWVAWAQCHGQGS (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_032183"
FT CONFLICT 173
FT /note="N -> D (in Ref. 1; BAE37459)"
FT /evidence="ECO:0000305"
FT CONFLICT 183
FT /note="N -> Y (in Ref. 1; BAB29602)"
FT /evidence="ECO:0000305"
FT CONFLICT 233
FT /note="T -> P (in Ref. 1; BAB32357)"
FT /evidence="ECO:0000305"
FT CONFLICT 375
FT /note="L -> V (in Ref. 1; BAB30158)"
FT /evidence="ECO:0000305"
FT MOD_RES A2AIW0-3:18
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 432 AA; 48025 MW; 7BFEF3179D254C9A CRC64;
MSGYARRQGA PPLSRTRSLV VPDAPAFYER RSCLPQLDCE RPHGGDLHPH LFGFRPTFMC
YVPSPVLASV GDTGFGYGKG KCTNQGPSGA PETRFGGDKL EDLEEANPFS FKEFLKTKNL
SLSKEDTTTS RIYPKEASRH PLGLEHSSPA SQLMGYGLES QQPFFEDPTR ASNLEEDEDD
GWNITYLPSA VDQTHSSRDT QDSPPCDTYL SFFSNSSELA CPESLPPWTL SDTDSRISPA
SPAGSPNADF AAHEESLGDR HLRTLQISYE ALKDENSKLR RKLNEVQSFS ETQTEMVRTL
ERKLEAKMIK EESDFHDLES VVQQVEQNLE LMTKRAVKAE NHVLKLKQEI NLLQAQLSNL
RRENEALRSG QGASLSVVKQ NTDVALQNLH LVMNSAHASI KQLVSGADTL NLVAEILKSI
DRISEVKDEV DS
