EH1L1_MOUSE
ID EH1L1_MOUSE Reviewed; 1716 AA.
AC Q99MS7; Q3V443; Q8C2W6; Q99J97; Q99MS5; Q99MS6;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 114.
DE RecName: Full=EH domain-binding protein 1-like protein 1;
DE AltName: Full=Tangerin;
GN Name=Ehbp1l1;
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; 3; 4 AND 5).
RC STRAIN=BALB/cJ;
RA Melichar J.M., Noegel A.A., Korenbaum E.;
RT "Tangerin, a novel Golgi-associated protein with calponin-homology domain
RT and CAAX-box.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 155-1716 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Ovary;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1444 AND SER-1460, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-278; THR-448; SER-1074 AND
RP SER-1444, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Lung, and Spleen;
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 FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH RAB8A; RAB8B; RAB10;
RP RAB13; BIN1; AMPH AND DNM1.
RX PubMed=26833786; DOI=10.1083/jcb.201508086;
RA Nakajo A., Yoshimura S., Togawa H., Kunii M., Iwano T., Izumi A.,
RA Noguchi Y., Watanabe A., Goto A., Sato T., Harada A.;
RT "EHBP1L1 coordinates Rab8 and Bin1 to regulate apical-directed transport in
RT polarized epithelial cells.";
RL J. Cell Biol. 212:297-306(2016).
CC -!- FUNCTION: May act as Rab effector protein and play a role in vesicle
CC trafficking (By similarity). Involved in apical-directed transport in
CC polarized epithelial cells; the functions seems to implicate Rab8, BIN1
CC and possibly DNM1 (PubMed:26833786). {ECO:0000250|UniProtKB:Q8N3D4}.
CC -!- SUBUNIT: Interacts with RAB8A, RAB8B, RAB10, RAB13 and RAB15 (in their
CC GTP-bound forms); at least in case of RAB8A can bind 2 molecules of
CC RAB8A simultaneously. Interacts with BIN1 and AMPH. Interacts with
CC DNM1. {ECO:0000250|UniProtKB:Q8N3D4, ECO:0000269|PubMed:26833786}.
CC -!- SUBCELLULAR LOCATION: Endosome {ECO:0000250|UniProtKB:Q8N3D4}.
CC Recycling endosome {ECO:0000269|PubMed:26833786}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=Tangerin A;
CC IsoId=Q99MS7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99MS7-2; Sequence=VSP_024839, VSP_024840;
CC Name=3; Synonyms=Tangerin B;
CC IsoId=Q99MS7-3; Sequence=VSP_024839;
CC Name=4; Synonyms=Tangerin C;
CC IsoId=Q99MS7-4; Sequence=VSP_024838;
CC Name=5; Synonyms=Tangerin C';
CC IsoId=Q99MS7-5; Sequence=VSP_024837, VSP_024838;
CC -!- DOMAIN: The CAAX motif is a signal for prenylation and required for
CC endosomal colocalization with Rab8 and Rab10.
CC {ECO:0000250|UniProtKB:Q8N3D4}.
CC -!- DOMAIN: The bivalent Mical/EHBP Rab binding (bMERB) domain, mediates
CC binding to Rab8, Rab10, Rab10, Rab13 and Rab15 (in their GTP-bound
CC forms). {ECO:0000250|UniProtKB:Q8N3D4}.
CC -!- PTM: Prenylated (Probable). Farnelysation (predominant) and
CC geranylgeranylation has been observed in vitro.
CC {ECO:0000250|UniProtKB:Q8N3D4}.
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; AF305087; AAK32109.1; -; mRNA.
DR EMBL; AF305088; AAK32110.1; -; mRNA.
DR EMBL; AF305089; AAK32111.1; -; mRNA.
DR EMBL; AF305090; AAK32112.1; -; mRNA.
DR EMBL; BC004660; AAH04660.1; -; mRNA.
DR EMBL; AK087817; BAC40012.1; -; mRNA.
DR EMBL; AK013080; BAE43236.1; -; mRNA.
DR CCDS; CCDS89316.1; -. [Q99MS7-2]
DR RefSeq; NP_444482.2; NM_053252.3.
DR AlphaFoldDB; Q99MS7; -.
DR SMR; Q99MS7; -.
DR BioGRID; 227759; 11.
DR STRING; 10090.ENSMUSP00000037656; -.
DR iPTMnet; Q99MS7; -.
DR PhosphoSitePlus; Q99MS7; -.
DR EPD; Q99MS7; -.
DR jPOST; Q99MS7; -.
DR MaxQB; Q99MS7; -.
DR PaxDb; Q99MS7; -.
DR PeptideAtlas; Q99MS7; -.
DR PRIDE; Q99MS7; -.
DR ProteomicsDB; 277807; -. [Q99MS7-1]
DR ProteomicsDB; 277808; -. [Q99MS7-2]
DR ProteomicsDB; 277809; -. [Q99MS7-3]
DR ProteomicsDB; 277810; -. [Q99MS7-4]
DR ProteomicsDB; 277811; -. [Q99MS7-5]
DR DNASU; 114601; -.
DR GeneID; 114601; -.
DR KEGG; mmu:114601; -.
DR UCSC; uc008gev.2; mouse. [Q99MS7-2]
DR CTD; 254102; -.
DR MGI; MGI:3612340; Ehbp1l1.
DR eggNOG; KOG0035; Eukaryota.
DR InParanoid; Q99MS7; -.
DR PhylomeDB; Q99MS7; -.
DR BioGRID-ORCS; 114601; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Ehbp1l1; mouse.
DR PRO; PR:Q99MS7; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q99MS7; protein.
DR GO; GO:0031941; C:filamentous actin; IBA:GO_Central.
DR GO; GO:0005815; C:microtubule organizing center; IBA:GO_Central.
DR GO; GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR CDD; cd00014; CH; 1.
DR Gene3D; 1.10.418.10; -; 1.
DR InterPro; IPR022735; bMERB_dom.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR029928; Ehbp1l1.
DR InterPro; IPR019448; NT-C2.
DR PANTHER; PTHR23167:SF42; PTHR23167:SF42; 1.
DR Pfam; PF00307; CH; 1.
DR Pfam; PF12130; DUF3585; 1.
DR Pfam; PF10358; NT-C2; 1.
DR SMART; SM00033; CH; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR PROSITE; PS51848; BMERB; 1.
DR PROSITE; PS51840; C2_NT; 1.
DR PROSITE; PS50021; CH; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Endosome; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1716
FT /note="EH domain-binding protein 1-like protein 1"
FT /id="PRO_0000285205"
FT DOMAIN 8..157
FT /note="C2 NT-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01186"
FT DOMAIN 1211..1316
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 1542..1694
FT /note="bMERB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01195"
FT REGION 174..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 598..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1173..1210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1382..1543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1399..1549
FT /note="Interaction with BIN1 and AMPH"
FT /evidence="ECO:0000269|PubMed:26833786"
FT COILED 1005..1033
FT /evidence="ECO:0000255"
FT COILED 1558..1707
FT /evidence="ECO:0000255"
FT MOTIF 1713..1716
FT /note="CAAX motif"
FT /evidence="ECO:0000250|UniProtKB:Q8N3D4"
FT COMPBIAS 209..231
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..386
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..430
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..497
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..542
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..559
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1461..1475
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1512..1534
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 170
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N3D4"
FT MOD_RES 173
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N3D4"
FT MOD_RES 191
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N3D4"
FT MOD_RES 278
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 310
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N3D4"
FT MOD_RES 367
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N3D4"
FT MOD_RES 424
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N3D4"
FT MOD_RES 448
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1074
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1135
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N3D4"
FT MOD_RES 1342
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N3D4"
FT MOD_RES 1444
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1460
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT VAR_SEQ 211
FT /note="S -> SGRGCAPRLGRFP (in isoform 5)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_024837"
FT VAR_SEQ 249..1205
FT /note="Missing (in isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_024838"
FT VAR_SEQ 365..1206
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|Ref.1"
FT /id="VSP_024839"
FT VAR_SEQ 1438
FT /note="V -> VSGV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024840"
FT CONFLICT 155
FT /note="G -> W (in Ref. 3; BAC40012)"
FT /evidence="ECO:0000305"
FT CONFLICT 364
FT /note="V -> A (in Ref. 1; AAK32110, 2; AAH04660 and 3;
FT BAC40012)"
FT /evidence="ECO:0000305"
FT CONFLICT 1522
FT /note="V -> A (in Ref. 3; BAC40012)"
FT /evidence="ECO:0000305"
FT CONFLICT 1544
FT /note="A -> T (in Ref. 3; BAC40012)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1716 AA; 184834 MW; CE9587BAAD06CA00 CRC64;
MTSVWKRLQR VGKRAAKFQF VACYHELVLE CTKKWQPDKL VVVWTRRNRR ICSKAHSWQP
GIQNPYRGTV VWMVPENVDI SVTLYRDPHV DQYETKEWTF IIENESKGQR KVLATVDVNL
AHHAGPVPAQ VPLRLRLKPK SVKVVHAELS LTLSGVLLRE GRATDDDMQS LASLMSVKPS
DVGNLDDFAE SDEEEANGPG APEVRTRGPQ SDLSRELKTL CEEEDEGHIR PQQAAARPSS
AEDTSPAPVS APAPPVRAFR GQGSEPAAIT GGQVGPETPE PPPSPPETRS TGQPGQTMVP
TPAPRLRKGS DAPSSPVPCS GDEVPNTSED PPTGMGSSGE TQAQISSQEG TEAHEARPEP
DIEVRGSKDS LGGERSKVEE EERGDGPGAS GTGNREKNTK KSDTTAGEAG ESSELHQVDA
EHKSKVQHRA TEGPEAAGLT PKARLGDTPE APPRSAQRRM GVRTQEEAPS DLNPPPAEPE
EHLGDLRDAR PAGQEKGSAE VRSKVPAIGR AGPEQGSSAR AASAGPQVSC VQTVPSDGQG
VKSRDQRAQE AEVGESRVLE TEAEWVPWEV IGTSKTDAGI PESLDTEAGT AESEILEAQE
SEAARSEGLE PEAAGTAESE VLRTQNNEIV VLGMPRTGPE IREPEEFGET EVGGFTVPDT
KTVIAETEIL ETQGVVDGEA AVLKTQAEIS ETQKTEAGEA EAGTLESQKV AAEGLGAPEV
GAEMAEAEKL GVQETEVEIW RIPRIETETA GTETLGIHKI GPPQMQPRLV GDQETDVSVM
ETAEDAILGT REITAGCGVL LIEAKIPESK IDRSLETEEG DLGVLEVDTG IAEAKILGIP
ERAPGVQKAL GAGTEVARVL EAEAASSEVP ETDAEEAETL QAKERSESSV ALRVVANLPE
SELLGTQKTE VGGTGISQRE VREAETEIPK TQEISSEGSG VPDLEAKMEE SGRKMEIWET
PEVEKVNSEL FGTQKGSEIP ELETKTIKSE ILDAQETEVR DLGLRRGEAE KAEAEMLETQ
KMEAKTARDE EIELVDPGVS SPEAEALRVQ WAGTVVLESG EVKADILGVQ KPGSWGALKY
EALDVPVTKQ RLSGAKEVVP EVPRAQEPET KVLGIVEAKS WTLGQQEAEM EGFESPENKS
NIFEAQEADS GVLGTMKGKE AVESLEEAGL SKAQVASEAG AGVPRPSGAS SLEEPEEDRR
LPGSQAPPTL VSSSQSLLEW CQEVTNGYRG VCITNFTTSW RNGLAFCAIL HRFYPDKIDY
FSLDPLNIKQ NNKQAFDGFA ALGVSRLLEP ADMVLLSVPD KLIVMTYLCQ IRAFCTGQEL
QLVQLEGGGG SGTYRVGNAQ PSLPDCLDAG DLAQRLREHG AEVPTEPKEA VNRGTGAIPK
VASRDTDLSC SSKDGEAEVA QEAIPQEAPT DGPRARSSTT PVVPAEGLVN GVGASGGVRL
RRSSVNGEAG PVPPPRAHGS FSHVRDADLL KKRRSRLRNS NSFSVDDQDS GAAVGAGPAG
PGAVEGPNPA SSPDANPLPA PVPQQPPGGP PPTEESSPSL GEEAGLQRFQ DTSQYVCAEL
QALEQEQGQI DGRAAEVEKQ LRSLMESGAN RLQEEVLIQE WFTLVNKKNA LIRRQDQLQL
LIEEQDLERR FELLSRELRA MLAIEEWQKT VAQQHREQLL LEELVSLVNQ RDELVRDLDQ
KERIALEEDE RLERGLEQRR RKVSRQLSRR ERCTLS
