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Q9R045 (ANGL2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 101. 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:
Angiopoietin-related protein 2
Alternative name(s):
Angiopoietin-like protein 2
Gene names
Name:Angptl2
Synonyms:Arp2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length493 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Induces sprouting in endothelial cells through an autocrine and paracrine action By similarity.

Subcellular location

Secreted By similarity.

Tissue specificity

Widely expressed in heart, tongue, lung and skeletal muscle. Also found in lower levels in kidney, epididymis and testis.

Sequence similarities

Contains 1 fibrinogen C-terminal domain.

Ontologies

Keywords
   Cellular componentSecreted
   DomainCoiled coil
Signal
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 493474Angiopoietin-related protein 2
PRO_0000009121

Regions

Domain269 – 489221Fibrinogen C-terminal
Coiled coil77 – 11539 Potential
Coiled coil152 – 20251 Potential

Amino acid modifications

Glycosylation1641N-linked (GlcNAc...) Potential
Glycosylation1921N-linked (GlcNAc...) Potential
Disulfide bond278 ↔ 307 By similarity
Disulfide bond430 ↔ 443 By similarity

Experimental info

Sequence conflict490 – 4912NT → DI in AAD55358. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9R045 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 22884B4010746BF2

FASTA49357,105
        10         20         30         40         50         60 
MRPLCMTYWW LGLLATVGAA TGPEADVEGT EDGSQREYIY LNRYKRAGES PDKCTYTFIV 

        70         80         90        100        110        120 
PQQRVTGAIC VNSKEPEVHL ENRVHKQELE LLNNELLKQK RQIETLQQLV EVDGGIVSEV 

       130        140        150        160        170        180 
KLLRKESRNM NSRVTQLYMQ LLHEIIRKRD NALELSQLEN RILNQTADML QLASKYKDLE 

       190        200        210        220        230        240 
HKFQHLAMLA HNQSEVIAQL EEHCQRVPAA RPMPQPPPAA PPRVYQPPTY NRIINQISTN 

       250        260        270        280        290        300 
EIQSDQNLKV LPPSLPTMPA LTSLPSSTDK PSGPWRDCLQ ALEDGHSTSS IYLVKPENTN 

       310        320        330        340        350        360 
RLMQVWCDQR HDPGGWTVIQ RRLDGSVNFF RNWETYKQGF GNIDGEYWLG LENIYWLTNQ 

       370        380        390        400        410        420 
GNYKLLVTME DWSGRKVFAE YASFRLEPES EYYKLRLGRY HGNAGDSFTW HNGKQFTTLD 

       430        440        450        460        470        480 
RDHDVYTGNC AHYQKGGWWY NACAHSNLNG VWYRGGHYRS RYQDGVYWAE FRGGSYSLKK 

       490 
VVMMIRPNPN TFH 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning, expression, and characterization of angiopoietin-related protein. angiopoietin-related protein induces endothelial cell sprouting."
Kim I., Moon S.-O., Koh K.N., Kim H., Uhm C.-S., Kwak H.J., Kim N.-G., Koh G.Y.
J. Biol. Chem. 274:26523-26528(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Heart.
[2]"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 and NOD.
Tissue: Thymus.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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].
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF125176 mRNA. Translation: AAD55358.1.
AK037265 mRNA. Translation: BAC29780.1.
AK155464 mRNA. Translation: BAE33276.1.
AL845277 Genomic DNA. Translation: CAM22212.1.
CH466542 Genomic DNA. Translation: EDL08597.1.
BC138609 mRNA. Translation: AAI38610.1.
BC138610 mRNA. Translation: AAI38611.1.
CCDSCCDS15940.1.
RefSeqNP_036053.2. NM_011923.4.
XP_006498114.1. XM_006498051.1.
UniGeneMm.208919.

3D structure databases

ProteinModelPortalQ9R045.
SMRQ9R045. Positions 248-487.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204920. 1 interaction.

PTM databases

PhosphoSiteQ9R045.

Proteomic databases

PaxDbQ9R045.
PRIDEQ9R045.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000004208; ENSMUSP00000004208; ENSMUSG00000004105.
GeneID26360.
KEGGmmu:26360.
UCSCuc008jhq.1. mouse.

Organism-specific databases

CTD23452.
MGIMGI:1347002. Angptl2.

Phylogenomic databases

eggNOGNOG251988.
GeneTreeENSGT00740000114872.
HOGENOMHOG000037129.
HOVERGENHBG103336.
InParanoidQ8BM09.
OMAEEHCQRV.
OrthoDBEOG7X9G60.
TreeFamTF336658.

Gene expression databases

BgeeQ9R045.
CleanExMM_ANGPTL2.
GenevestigatorQ9R045.

Family and domain databases

Gene3D3.90.215.10. 1 hit.
4.10.530.10. 1 hit.
InterProIPR014716. Fibrinogen_a/b/g_C_1.
IPR014715. Fibrinogen_a/b/g_C_2.
IPR002181. Fibrinogen_a/b/g_C_dom.
IPR020837. Fibrinogen_CS.
[Graphical view]
PfamPF00147. Fibrinogen_C. 1 hit.
[Graphical view]
SMARTSM00186. FBG. 1 hit.
[Graphical view]
SUPFAMSSF56496. SSF56496. 1 hit.
PROSITEPS00514. FIBRINOGEN_C_1. 1 hit.
PS51406. FIBRINOGEN_C_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio304215.
PROQ9R045.
SOURCESearch...

Entry information

Entry nameANGL2_MOUSE
AccessionPrimary (citable) accession number: Q9R045
Secondary accession number(s): Q8BM09
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 101 of the entry and version 2 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