MAP7_MOUSE
ID MAP7_MOUSE Reviewed; 730 AA.
AC O88735; Q3V0B9; Q7TQL9; Q80V60;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Ensconsin;
DE AltName: Full=Epithelial microtubule-associated protein of 115 kDa;
DE Short=E-MAP-115;
DE AltName: Full=Microtubule-associated protein 7;
DE Short=MAP-7;
GN Name=Map7; Synonyms=Mtap7;
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] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=C57BL/6 X CBA;
RX PubMed=9745708; DOI=10.1111/j.1432-0436.1998.00169.x;
RA Fabre-Jonca N., Allaman J.-M., Radlgruber G., Meda P., Kiss J.Z.,
RA French L.E., Masson D.;
RT "The distribution of murine 115-kDa epithelial microtubule-associated
RT protein (E-MAP-115) during embryogenesis and in adult organs suggests a
RT role in epithelial polarization and differentiation.";
RL Differentiation 63:169-180(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND INTERACTION WITH TRPV4.
RC TISSUE=Kidney;
RX PubMed=14517216; DOI=10.1074/jbc.m308212200;
RA Suzuki M., Hirao A., Mizuno A.;
RT "Microtubule-associated protein 7 increases the membrane expression of
RT transient receptor potential vanilloid 4 (TRPV4).";
RL J. Biol. Chem. 278:51448-51453(2003).
RN [3]
RP ERRATUM OF PUBMED:14517216.
RA Suzuki M., Hirao A., Mizuno A.;
RL J. Biol. Chem. 280:25948-25948(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-494 (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Eye, and Mammary gland;
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 [6]
RP TISSUE SPECIFICITY.
RX PubMed=12755995; DOI=10.1046/j.1365-2605.2003.00406.x;
RA Penttilae T.-L., Parvinen M., Paranko J.;
RT "Microtubule-associated epithelial protein E-MAP-115 is localized in the
RT spermatid manchette.";
RL Int. J. Androl. 26:166-174(2003).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202 AND SER-209, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, Lung, Pancreas, 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).
CC -!- FUNCTION: Microtubule-stabilizing protein that may play an important
CC role during reorganization of microtubules during polarization and
CC differentiation of epithelial cells. Associates with microtubules in a
CC dynamic manner. May play a role in the formation of intercellular
CC contacts. Colocalization with TRPV4 results in the redistribution of
CC TRPV4 toward the membrane and may link cytoskeletal microfilaments.
CC {ECO:0000269|PubMed:14517216}.
CC -!- SUBUNIT: Interacts with TRPV4. {ECO:0000269|PubMed:14517216}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:14517216}. Basolateral cell membrane
CC {ECO:0000269|PubMed:14517216}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:14517216}. Note=Colocalized on microtubules. An
CC intracellular redistribution is triggered during induction of
CC keratinocyte terminal differentiation from microtubules with a
CC perinuclear localization to cortical microtubules organized in spike-
CC like bundles facing intercellular contacts.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O88735-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O88735-2; Sequence=VSP_021318;
CC -!- TISSUE SPECIFICITY: Highly expressed in the epithelial cells of the
CC kidney tubules and in the absorptive cells of the intestine, and widely
CC distributed in the testis. Expression correlates with the
CC differentiation of certain epithelial cell types: in the adult
CC intestine, more abundantly expressed in the differentiating than in the
CC proliferative cell compartment. The expression clearly correlates with
CC the degree of cellular apicobasal polarity. Expressed in lung, kidney,
CC brain and fat. Colocalized with TRPV4 in ependymal cells, in the
CC choroid plexus, in bronchial and renal cortical tubular cells. Widely
CC expressed in excitable neuronal cells, vascular cells as well as in
CC epithelial cells. In seminiferous epithelium, associated with the
CC microtubule of the spermatid manchette. {ECO:0000269|PubMed:12755995,
CC ECO:0000269|PubMed:14517216, ECO:0000269|PubMed:9745708}.
CC -!- DEVELOPMENTAL STAGE: Expressed in several epithelia from 9.5 dpc
CC onwards, with expression levels increasing during development. From
CC 14.5 dpc onwards, found in some neuronal cells as well.
CC {ECO:0000269|PubMed:9745708}.
CC -!- PTM: The association with microtubules is regulated by phosphorylation
CC during the cell cycle. During interphase only phosphorylated on serine.
CC Phosphorylated on threonine in mitosis (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MAP7 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH42771.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; 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; Y15197; CAA75495.1; -; mRNA.
DR EMBL; AB098611; BAC53729.1; -; mRNA.
DR EMBL; AK133267; BAE21585.1; -; mRNA.
DR EMBL; BC042771; AAH42771.1; ALT_SEQ; mRNA.
DR EMBL; BC052637; AAH52637.1; -; mRNA.
DR CCDS; CCDS56694.1; -. [O88735-2]
DR CCDS; CCDS87968.1; -. [O88735-1]
DR RefSeq; NP_001185564.1; NM_001198635.1.
DR RefSeq; NP_032661.2; NM_008635.2.
DR AlphaFoldDB; O88735; -.
DR SMR; O88735; -.
DR BioGRID; 201588; 2.
DR IntAct; O88735; 1.
DR MINT; O88735; -.
DR STRING; 10090.ENSMUSP00000111963; -.
DR iPTMnet; O88735; -.
DR PhosphoSitePlus; O88735; -.
DR MaxQB; O88735; -.
DR PaxDb; O88735; -.
DR PeptideAtlas; O88735; -.
DR PRIDE; O88735; -.
DR ProteomicsDB; 295820; -. [O88735-1]
DR ProteomicsDB; 295821; -. [O88735-2]
DR DNASU; 17761; -.
DR GeneID; 17761; -.
DR KEGG; mmu:17761; -.
DR UCSC; uc007eno.2; mouse. [O88735-1]
DR CTD; 9053; -.
DR MGI; MGI:1328328; Map7.
DR eggNOG; ENOG502QTDQ; Eukaryota.
DR InParanoid; O88735; -.
DR OrthoDB; 738080at2759; -.
DR PhylomeDB; O88735; -.
DR BioGRID-ORCS; 17761; 5 hits in 71 CRISPR screens.
DR ChiTaRS; Map7; mouse.
DR PRO; PR:O88735; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; O88735; protein.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0005102; F:signaling receptor binding; IPI:BHF-UCL.
DR GO; GO:0000902; P:cell morphogenesis; IMP:MGI.
DR GO; GO:0008283; P:cell population proliferation; IMP:MGI.
DR GO; GO:0009566; P:fertilization; IMP:MGI.
DR GO; GO:0007281; P:germ cell development; IMP:MGI.
DR GO; GO:0006687; P:glycosphingolipid metabolic process; IMP:MGI.
DR GO; GO:0048872; P:homeostasis of number of cells; IMP:MGI.
DR GO; GO:0033327; P:Leydig cell differentiation; IMP:MGI.
DR GO; GO:0001578; P:microtubule bundle formation; IMP:MGI.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0006997; P:nucleus organization; IMP:MGI.
DR GO; GO:0035265; P:organ growth; IMP:MGI.
DR GO; GO:0072659; P:protein localization to plasma membrane; IDA:BHF-UCL.
DR GO; GO:0006970; P:response to osmotic stress; IDA:BHF-UCL.
DR GO; GO:0032526; P:response to retinoic acid; IMP:MGI.
DR GO; GO:0060009; P:Sertoli cell development; IMP:MGI.
DR GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR InterPro; IPR030707; MAP7.
DR InterPro; IPR008604; MAP7_fam.
DR PANTHER; PTHR15073:SF4; PTHR15073:SF4; 1.
DR Pfam; PF05672; MAP7; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell membrane; Coiled coil; Cytoplasm;
KW Cytoskeleton; Isopeptide bond; Membrane; Microtubule; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q14244"
FT CHAIN 2..730
FT /note="Ensconsin"
FT /id="PRO_0000255950"
FT REGION 1..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 403..669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 89..152
FT /evidence="ECO:0000255"
FT COILED 460..589
FT /evidence="ECO:0000255"
FT COMPBIAS 34..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..155
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..307
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..388
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..437
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..459
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..608
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 632..669
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q14244"
FT MOD_RES 161
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14244"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14244"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14244"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 209
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 219
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14244"
FT MOD_RES 231
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14244"
FT MOD_RES 235
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14244"
FT MOD_RES 254
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14244"
FT MOD_RES 277
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14244"
FT MOD_RES 282
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14244"
FT MOD_RES 336
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14244"
FT MOD_RES 366
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14244"
FT CROSSLNK 273
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14244"
FT CROSSLNK 295
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14244"
FT CROSSLNK 374
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14244"
FT CROSSLNK 378
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14244"
FT CROSSLNK 398
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14244"
FT VAR_SEQ 250
FT /note="T -> TVIPICPRS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_021318"
FT CONFLICT 4
FT /note="Q -> H (in Ref. 4; BAE21585)"
FT /evidence="ECO:0000305"
FT CONFLICT 8
FT /note="G -> C (in Ref. 4; BAE21585)"
FT /evidence="ECO:0000305"
FT CONFLICT 16
FT /note="G -> S (in Ref. 4; BAE21585)"
FT /evidence="ECO:0000305"
FT CONFLICT 35
FT /note="A -> G (in Ref. 4; BAE21585)"
FT /evidence="ECO:0000305"
FT CONFLICT 360
FT /note="A -> T (in Ref. 5; AAH42771)"
FT /evidence="ECO:0000305"
FT CONFLICT 373
FT /note="F -> V (in Ref. 4; BAE21585 and 5; AAH52637/
FT AAH42771)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 730 AA; 82022 MW; F44B4201DE8F5A17 CRC64;
MAEQGAGGDG HRGGDGATHS DPASDGYKVQ EKRTAPSRPT STVSGQTSNH SGNKPDPPPV
LRVDDRQRLA RERREEREKQ LAARETVWLE REERARQHYE RHLEARKKKL EDQRLKEERR
RAAVEEKRRQ RLEEDKERHE AVVRRTMERS QKPRQKSNRW SWGSPLHGSS SIHSGDPDRR
SVSTMNLSKH VDPVISKRLS SSSATLLNSP DRARRLQLSP WESSVVSRLL TPTHSFLARS
KSTAALSGDT ASCSPIIMPF KAAHSRNPVD RPKLFVTPPE GSARRRTIHG LASHKRERER
EHVPFHVSPG ARRTLSPSNL KARSPAPARL WLPSKSMPHL PGTPRPASSL PPGSVRAASA
QAPSSSPGNI RPFKREVKVE PEKKDPLPAV KSRVPLVKVE EVTVEEGTPV KPPEPAAPAS
APIATPAPAP ATDPAPVPAP SSTVTVGVVP KTSAGTTDPE EATRLLAEKR RLAREQREKE
ERERKEKEEL ERQKIEELAR RVAEERSRRE EEARRLEEEQ AREKEELALR LAEEERERWE
REEVERVQKQ KEEEARAREE AERARQEREK HFQKEEQERL ERKKRLEEIM RRTRRTETAD
KKTTEQRNGD IAKGVLTGEP EVPALPCMAS SGNGESAESP HGVALQQSEV TTESSPDLEK
QPNENGMSIQ NENFEEVINL PVGSKASRLD VTNENPEIPL KPILAFNDEG TLGPLPQVDG
VQTQQTAEVI
