Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q64299 (NOV_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 107. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein NOV homolog

Short name=NovH
Alternative name(s):
CCN family member 3
Nephroblastoma-overexpressed gene protein homolog
Gene names
Name:Nov
Synonyms:Ccn3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length354 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Immediate-early protein likely to play a role in cell growth regulation By similarity.

Subunit structure

Interacts with FBLN1 By similarity.

Subcellular location

Secreted.

Sequence similarities

Belongs to the CCN family.

Contains 1 CTCK (C-terminal cystine knot-like) domain.

Contains 1 IGFBP N-terminal domain.

Contains 1 TSP type-1 domain.

Contains 1 VWFC domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 354333Protein NOV homolog
PRO_0000014416

Regions

Domain25 – 9975IGFBP N-terminal
Domain102 – 16867VWFC
Domain202 – 24746TSP type-1
Domain261 – 33575CTCK

Amino acid modifications

Glycosylation911N-linked (GlcNAc...) Potential
Glycosylation2771N-linked (GlcNAc...) Potential
Disulfide bond261 ↔ 298 By similarity
Disulfide bond278 ↔ 312 By similarity
Disulfide bond289 ↔ 328 By similarity
Disulfide bond292 ↔ 330 By similarity
Disulfide bond297 ↔ 334 By similarity

Experimental info

Sequence conflict61R → G in BAC30363. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q64299 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 08ECE8CFC67829DE

FASTA35438,928
        10         20         30         40         50         60 
MSLFLRKRCL CLGFLLFHLL SQVSASLRCP SRCPPKCPSI SPTCAPGVRS VLDGCSCCPV 

        70         80         90        100        110        120 
CARQRGESCS EMRPCDQSSG LYCDRSADPN NQTGICMVPE GDNCVFDGVI YRNGEKFEPN 

       130        140        150        160        170        180 
CQYFCTCRDG QIGCLPRCQL DVLLPGPDCP APRKVAVPGE CCEKWTCGSD EQGTQGTLGG 

       190        200        210        220        230        240 
LALPAYRPEA TVGVEVSDSS INCIEQTTEW SACSKSCGMG VSTRVTNRNR QCEMVKQTRL 

       250        260        270        280        290        300 
CIVRPCEQEP EEVTDKKGKK CLRTKKSLKA IHLQFENCTS LYTYKPRFCG VCSDGRCCTP 

       310        320        330        340        350 
HNTKTIQVEF QCLPGEIIKK PVMVIGTCTC YSNCPQNNEA FLQDLELKTS RGEI 

« Hide

References

« Hide 'large scale' references
[1]"Genomic structure and chromosomal mapping of the mouse nov gene."
Snaith M.R., Natarajan D., Taylor L.B., Choi C.P., Martinerie C., Perbal B., Schofield P.N., Boulter C.A.
Genomics 38:425-428(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Strain: 129/Sv and ICR.
Tissue: Brain.
[2]"Regulation of nov by WT1: a potential role for nov in nephrogenesis."
Martinerie C., Chevalier G., Rauscher F.J. III, Perbal B.
Oncogene 12:1479-1492(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6.
[3]"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].
Strain: C57BL/6J.
Tissue: Embryonic head and Spinal cord.
[4]"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].
Strain: Czech II.
Tissue: Mammary tumor.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X97863 Genomic DNA. Translation: CAA66457.1.
Y09257 mRNA. Translation: CAA70454.1.
X96585 mRNA. Translation: CAA65404.1.
AK039481 mRNA. Translation: BAC30363.1.
AK081944 mRNA. Translation: BAC38378.1.
BC003774 mRNA. Translation: AAH03774.1.
CCDSCCDS27471.1.
RefSeqNP_035060.1. NM_010930.4.
UniGeneMm.5167.

3D structure databases

ProteinModelPortalQ64299.
SMRQ64299. Positions 270-335.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000054389.

Proteomic databases

PaxDbQ64299.
PRIDEQ64299.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000050027; ENSMUSP00000054389; ENSMUSG00000037362.
GeneID18133.
KEGGmmu:18133.
UCSCuc007vrn.1. mouse.

Organism-specific databases

CTD4856.
MGIMGI:109185. Nov.

Phylogenomic databases

eggNOGNOG72934.
GeneTreeENSGT00750000117442.
HOGENOMHOG000231462.
HOVERGENHBG000635.
InParanoidQ64299.
OMACCTPHNT.
OrthoDBEOG7N8ZXB.
PhylomeDBQ64299.
TreeFamTF326070.

Gene expression databases

BgeeQ64299.
CleanExMM_NOV.
GenevestigatorQ64299.

Family and domain databases

InterProIPR006207. Cys_knot_C.
IPR006208. Glyco_hormone_CN.
IPR009030. Growth_fac_rcpt_N_dom.
IPR000867. IGFBP-like.
IPR012395. IGFBP_CNN.
IPR017891. Insulin_GF-bd_Cys-rich_CS.
IPR000884. Thrombospondin_1_rpt.
IPR001007. VWF_C.
[Graphical view]
PfamPF00007. Cys_knot. 1 hit.
PF00219. IGFBP. 1 hit.
PF00090. TSP_1. 1 hit.
PF00093. VWC. 1 hit.
[Graphical view]
PIRSFPIRSF036495. IGFBP_rP_CNN. 1 hit.
SMARTSM00041. CT. 1 hit.
SM00121. IB. 1 hit.
SM00209. TSP1. 1 hit.
SM00214. VWC. 1 hit.
[Graphical view]
SUPFAMSSF57184. SSF57184. 1 hit.
SSF82895. SSF82895. 1 hit.
PROSITEPS01185. CTCK_1. 1 hit.
PS01225. CTCK_2. 1 hit.
PS00222. IGFBP_N_1. 1 hit.
PS51323. IGFBP_N_2. 1 hit.
PS50092. TSP1. 1 hit.
PS01208. VWFC_1. 1 hit.
PS50184. VWFC_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio293376.
PROQ64299.
SOURCESearch...

Entry information

Entry nameNOV_MOUSE
AccessionPrimary (citable) accession number: Q64299
Secondary accession number(s): Q8CA67
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 107 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