O88735 (MAP7_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ensconsin

Alternative name(s):
Epithelial microtubule-associated protein of 115 kDa
Short name=E-MAP-115
Microtubule-associated protein 7
Short name=MAP-7

Gene names

Name:	Map7
Synonyms:	Mtap7

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	730 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Microtubule-stabilizing protein that may play an important role during reorganization of microtubules during polarization and differentiation of epithelial cells. Associates with microtubules in a dynamic manner. May play a role in the formation of intercellular contacts. Colocalization with TRPV4 results in the redistribution of TRPV4 toward the membrane and may link cytoskeletal microfilaments. Ref.2
Subunit structure	Interacts with TRPV4. Ref.2
Subcellular location	Cytoplasm › perinuclear region. Basolateral cell membrane. Cytoplasm › cytoskeleton. Note: Colocalized on microtubules. An intracellular redistribution is triggered during induction of keratinocyte terminal differentiation from microtubules with a perinuclear localization to cortical microtubules organized in spike-like bundles facing intercellular contacts. Ref.2
Tissue specificity	Highly expressed in the epithelial cells of the kidney tubules and in the absorptive cells of the intestine, and widely distributed in the testis. Expression correlates with the differentiation of certain epithelial cell types: in the adult intestine, more abundantly expressed in the differentiating than in the proliferative cell compartment. The expression clearly correlates with the degree of cellular apicobasal polarity. Expressed in lung, kidney, brain and fat. Colocalized with TRPV4 in ependymal cells, in the choroid plexus, in bronchial and renal cortical tubular cells. Widely expressed in excitable neuronal cells, vascular cells as well as in epithelial cells. In seminiferous epithelium, associated with the microtubule of the spermatid manchette. Ref.1 Ref.2 Ref.6
Developmental stage	Expressed in several epithelia from E9.5 onwards, with expression levels increasing during development. From E14.5 onwards, found in some neuronal cells as well. Ref.1
Post-translational modification	The association with microtubules is regulated by phosphorylation during the cell cycle. During interphase only phosphorylated on serine. Phosphorylated on threonine in mitosis By similarity.
Sequence similarities	Belongs to the MAP7 family.
Sequence caution	The sequence AAH42771.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

Ontologies

Keywords
Cellular component	Cell membrane Cytoplasm Cytoskeleton Membrane Microtubule
Coding sequence diversity	Alternative splicing
Domain	Coiled coil
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Leydig cell differentiation Inferred from mutant phenotype PubMed 10837026. Source: MGI Sertoli cell development Inferred from mutant phenotype PubMed 10837026. Source: MGI cell morphogenesis Inferred from mutant phenotype PubMed 10837026. Source: MGI cell proliferation Inferred from mutant phenotype PubMed 10837026. Source: MGI fertilization Inferred from mutant phenotype PubMed 10837026. Source: MGI germ cell development Inferred from mutant phenotype PubMed 10837026. Source: MGI glycosphingolipid metabolic process Inferred from mutant phenotype PubMed 18308723. Source: MGI homeostasis of number of cells Inferred from mutant phenotype PubMed 10837026. Source: MGI microtubule bundle formation Inferred from mutant phenotype PubMed 10837026. Source: MGI nucleus organization Inferred from mutant phenotype PubMed 10837026. Source: MGI organ growth Inferred from mutant phenotype PubMed 10837026. Source: MGI protein localization to plasma membrane Inferred from direct assay Ref.2. Source: BHF-UCL response to osmotic stress Inferred from direct assay Ref.2. Source: BHF-UCL response to retinoic acid Inferred from mutant phenotype PubMed 10837026. Source: MGI spermatogenesis Inferred from mutant phenotype PubMed 10837026. Source: MGI
Cellular_component	basolateral plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell microtubule Inferred from electronic annotation. Source: UniProtKB-KW perinuclear region of cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from direct assay Ref.2. Source: MGI
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O88735-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: O88735-2)

The sequence of this isoform differs from the canonical sequence as follows:
     250-250: T → TVIPICPRS

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 730	730	Ensconsin		PRO_0000255950
Regions
	Coiled coil	89 – 152	64	Potential
	Coiled coil	460 – 589	130	Potential
Amino acid modifications
	Modified residue	183	1	Phosphoserine By similarity
	Modified residue	203	1	Phosphoserine Ref.7
	Modified residue	209	1	Phosphoserine By similarity
	Modified residue	219	1	Phosphoserine By similarity
	Modified residue	231	1	Phosphothreonine By similarity
	Modified residue	254	1	Phosphoserine By similarity
	Modified residue	277	1	Phosphothreonine By similarity
Natural variations
	Alternative sequence	250	1	T → TVIPICPRS in isoform 2.		VSP_021318
Experimental info
	Sequence conflict	4	1	Q → H in BAE21585. Ref.4
	Sequence conflict	8	1	G → C in BAE21585. Ref.4
	Sequence conflict	16	1	G → S in BAE21585. Ref.4
	Sequence conflict	35	1	A → G in BAE21585. Ref.4
	Sequence conflict	360	1	A → T in AAH42771. Ref.5
	Sequence conflict	373	1	F → V in BAE21585. Ref.4
	Sequence conflict	373	1	F → V in AAH52637. Ref.5
	Sequence conflict	373	1	F → V in AAH42771. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: F44B4201DE8F5A17	FASTA	730	82,022
	10 20 30 40 50 60 MAEQGAGGDG HRGGDGATHS DPASDGYKVQ EKRTAPSRPT STVSGQTSNH SGNKPDPPPV 70 80 90 100 110 120 LRVDDRQRLA RERREEREKQ LAARETVWLE REERARQHYE RHLEARKKKL EDQRLKEERR 130 140 150 160 170 180 RAAVEEKRRQ RLEEDKERHE AVVRRTMERS QKPRQKSNRW SWGSPLHGSS SIHSGDPDRR 190 200 210 220 230 240 SVSTMNLSKH VDPVISKRLS SSSATLLNSP DRARRLQLSP WESSVVSRLL TPTHSFLARS 250 260 270 280 290 300 KSTAALSGDT ASCSPIIMPF KAAHSRNPVD RPKLFVTPPE GSARRRTIHG LASHKRERER 310 320 330 340 350 360 EHVPFHVSPG ARRTLSPSNL KARSPAPARL WLPSKSMPHL PGTPRPASSL PPGSVRAASA 370 380 390 400 410 420 QAPSSSPGNI RPFKREVKVE PEKKDPLPAV KSRVPLVKVE EVTVEEGTPV KPPEPAAPAS 430 440 450 460 470 480 APIATPAPAP ATDPAPVPAP SSTVTVGVVP KTSAGTTDPE EATRLLAEKR RLAREQREKE 490 500 510 520 530 540 ERERKEKEEL ERQKIEELAR RVAEERSRRE EEARRLEEEQ AREKEELALR LAEEERERWE 550 560 570 580 590 600 REEVERVQKQ KEEEARAREE AERARQEREK HFQKEEQERL ERKKRLEEIM RRTRRTETAD 610 620 630 640 650 660 KKTTEQRNGD IAKGVLTGEP EVPALPCMAS SGNGESAESP HGVALQQSEV TTESSPDLEK 670 680 690 700 710 720 QPNENGMSIQ NENFEEVINL PVGSKASRLD VTNENPEIPL KPILAFNDEG TLGPLPQVDG 730 VQTQQTAEVI
	Isoform 2 [UniParc]. Checksum: 8CEAE46EE589C5EE	FASTA	738	82,888
	10 20 30 40 50 60 MAEQGAGGDG HRGGDGATHS DPASDGYKVQ EKRTAPSRPT STVSGQTSNH SGNKPDPPPV 70 80 90 100 110 120 LRVDDRQRLA RERREEREKQ LAARETVWLE REERARQHYE RHLEARKKKL EDQRLKEERR 130 140 150 160 170 180 RAAVEEKRRQ RLEEDKERHE AVVRRTMERS QKPRQKSNRW SWGSPLHGSS SIHSGDPDRR 190 200 210 220 230 240 SVSTMNLSKH VDPVISKRLS SSSATLLNSP DRARRLQLSP WESSVVSRLL TPTHSFLARS 250 260 270 280 290 300 KSTAALSGDT VIPICPRSAS CSPIIMPFKA AHSRNPVDRP KLFVTPPEGS ARRRTIHGLA 310 320 330 340 350 360 SHKREREREH VPFHVSPGAR RTLSPSNLKA RSPAPARLWL PSKSMPHLPG TPRPASSLPP 370 380 390 400 410 420 GSVRAASAQA PSSSPGNIRP FKREVKVEPE KKDPLPAVKS RVPLVKVEEV TVEEGTPVKP 430 440 450 460 470 480 PEPAAPASAP IATPAPAPAT DPAPVPAPSS TVTVGVVPKT SAGTTDPEEA TRLLAEKRRL 490 500 510 520 530 540 AREQREKEER ERKEKEELER QKIEELARRV AEERSRREEE ARRLEEEQAR EKEELALRLA 550 560 570 580 590 600 EEERERWERE EVERVQKQKE EEARAREEAE RARQEREKHF QKEEQERLER KKRLEEIMRR 610 620 630 640 650 660 TRRTETADKK TTEQRNGDIA KGVLTGEPEV PALPCMASSG NGESAESPHG VALQQSEVTT 670 680 690 700 710 720 ESSPDLEKQP NENGMSIQNE NFEEVINLPV GSKASRLDVT NENPEIPLKP ILAFNDEGTL 730 GPLPQVDGVQ TQQTAEVI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The distribution of murine 115-kDa epithelial microtubule-associated protein (E-MAP-115) during embryogenesis and in adult organs suggests a role in epithelial polarization and differentiation." Fabre-Jonca N., Allaman J.-M., Radlgruber G., Meda P., Kiss J.Z., French L.E., Masson D. Differentiation 63:169-180(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE. Strain: C57BL/6 X CBA.
[2]	"Microtubule-associated protein 7 increases the membrane expression of transient receptor potential vanilloid 4 (TRPV4)." Suzuki M., Hirao A., Mizuno A. J. Biol. Chem. 278:51448-51453(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH TRPV4. Tissue: Kidney.
[3]	Erratum Suzuki M., Hirao A., Mizuno A. J. Biol. Chem. 280:25948-25948(2005)
[4]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Strain: C57BL/6J. Tissue: Testis.
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-494 (ISOFORM 1). Strain: FVB/N. Tissue: Eye and Mammary gland.
[6]	"Microtubule-associated epithelial protein E-MAP-115 is localized in the spermatid manchette." Penttilae T.-L., Parvinen M., Paranko J. Int. J. Androl. 26:166-174(2003) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[7]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Y15197 mRNA. Translation: CAA75495.1. AB098611 mRNA. Translation: BAC53729.1. AK133267 mRNA. Translation: BAE21585.1. BC042771 mRNA. Translation: AAH42771.1. Sequence problems. BC052637 mRNA. Translation: AAH52637.1.
IPI	IPI00380510. IPI01008688.
RefSeq	NP_001185564.1. NM_001198635.1. NP_032661.2. NM_008635.2.
UniGene	Mm.20928.
3D structure databases
ProteinModelPortal	O88735.
ModBase	Search...
PTM databases
PhosphoSite	O88735.
Proteomic databases
PaxDb	O88735.
PRIDE	O88735.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	17761.
KEGG	mmu:17761.
UCSC	uc007eno.2. mouse. uc011xba.1. mouse.
Organism-specific databases
CTD	9053.
MGI	MGI:1328328. Map7.
Phylogenomic databases
eggNOG	NOG46082.
HOGENOM	HOG000231569.
HOVERGEN	HBG081952.
KO	K10433.
OrthoDB	EOG41NTN2.
Gene expression databases
CleanEx	MM_MTAP7.
Genevestigator	O88735.
GermOnline	ENSMUSG00000019996. Mus musculus.
Family and domain databases
InterPro	IPR008604. E-MAP-115. [Graphical view]
PANTHER	PTHR15073. PTHR15073. 1 hit.
Pfam	PF05672. MAP7. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	292449.
SOURCE	Search...

Entry information

Entry name

MAP7_MOUSE

Accession

Primary (citable) accession number: O88735
Secondary accession number(s): Q3V0B9, Q7TQL9, Q80V60

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2006
Last sequence update:	November 1, 1998
Last modified:	April 3, 2013
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program