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O88735 (MAP7_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length730 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

Cytoplasmperinuclear region. Basolateral cell membrane. Cytoplasmcytoskeleton. 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 componentCell membrane
Cytoplasm
Cytoskeleton
Membrane
Microtubule
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processLeydig 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_componentbasolateral 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

   Molecular_functionprotein binding

Inferred from physical interaction Ref.2. Source: MGI

receptor binding

Inferred from physical interaction Ref.2. Source: BHF-UCL

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 730729Ensconsin
PRO_0000255950

Regions

Coiled coil89 – 15264 Potential
Coiled coil460 – 589130 Potential

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue1831Phosphoserine By similarity
Modified residue2091Phosphoserine By similarity
Modified residue2191Phosphoserine By similarity
Modified residue2311Phosphothreonine By similarity
Modified residue2541Phosphoserine By similarity
Modified residue2771Phosphothreonine By similarity

Natural variations

Alternative sequence2501T → TVIPICPRS in isoform 2.
VSP_021318

Experimental info

Sequence conflict41Q → H in BAE21585. Ref.4
Sequence conflict81G → C in BAE21585. Ref.4
Sequence conflict161G → S in BAE21585. Ref.4
Sequence conflict351A → G in BAE21585. Ref.4
Sequence conflict3601A → T in AAH42771. Ref.5
Sequence conflict3731F → V in BAE21585. Ref.4
Sequence conflict3731F → V in AAH52637. Ref.5
Sequence conflict3731F → V in AAH42771. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: F44B4201DE8F5A17

FASTA73082,022
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 8CEAE46EE589C5EE
Show »

FASTA73882,888

References

« Hide '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. expand/collapse author list , 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.
+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.
CCDSCCDS56694.1. [O88735-2]
RefSeqNP_001185564.1. NM_001198635.1.
NP_032661.2. NM_008635.2.
UniGeneMm.20928.

3D structure databases

ProteinModelPortalO88735.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActO88735. 1 interaction.
MINTMINT-4105617.

PTM databases

PhosphoSiteO88735.

Proteomic databases

MaxQBO88735.
PaxDbO88735.
PRIDEO88735.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID17761.
KEGGmmu:17761.
UCSCuc007eno.2. mouse. [O88735-1]

Organism-specific databases

CTD9053.
MGIMGI:1328328. Map7.

Phylogenomic databases

eggNOGNOG46082.
HOGENOMHOG000231569.
HOVERGENHBG081952.
KOK10433.
PhylomeDBO88735.

Gene expression databases

CleanExMM_MTAP7.
GenevestigatorO88735.

Family and domain databases

InterProIPR008604. MAP7.
[Graphical view]
PANTHERPTHR15073. PTHR15073. 1 hit.
PfamPF05672. MAP7. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio292449.
PROO88735.
SOURCESearch...

Entry information

Entry nameMAP7_MOUSE
AccessionPrimary (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: July 9, 2014
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot