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Reviewed, UniProtKB/Swiss-Prot P48036 (ANXA5_MOUSE)

Last modified June 16, 2009. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Annexin A5
Alternative name(s):
    Annexin-5
    Annexin V
    Lipocortin V
    Endonexin II
    Calphobindin I
      Short name=CBP-I
    Placental anticoagulant protein I
      Short name=PAP-I
    Placental anticoagulant protein 4
      Short name=PP4
    Thromboplastin inhibitor
    Vascular anticoagulant-alpha
      Short name=VAC-alpha
    Anchorin CII
Gene names
Name: Anxa5
Synonyms: Anx5
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length319 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

This protein is an anticoagulant protein that acts as an indirect inhibitor of the thromboplastin-specific complex, which is involved in the blood coagulation cascade.

Subunit structure

Monomer. Binds ATRX and EIF5B By similarity.

Domain

A pair of annexin repeats may form one binding site for calcium and phospholipid.

Sequence similarities

Belongs to the annexin family.

Contains 4 annexin repeats.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Kcnma1Q084601EBI-1184119,EBI-1633915

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 319319Annexin A5
PRO_0000067488

Regions

Repeat22 – 8261Annexin 1
Repeat94 – 15461Annexin 2
Repeat178 – 23861Annexin 3
Repeat253 – 31361Annexin 4

Amino acid modifications

Modified residue921Phosphotyrosine By similarity
Modified residue991N6-acetyllysine By similarity

Experimental info

Sequence conflict1421D → G in BAE28107. Ref.4
Sequence conflict1571A → G in AAH03716. Ref.5
Sequence conflict2841K → N in BAE31952. Ref.4
Sequence conflict3001G → S in BAE32026. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P48036-1 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 55055BAF2E1C36B7

FASTA31935,752
        10         20         30         40         50         60 
MATRGTVTDF PGFDGRADAE VLRKAMKGLG TDEDSILNLL TSRSNAQRQE IAQEFKTLFG 

        70         80         90        100        110        120 
RDLVDDLKSE LTGKFEKLIV AMMKPSRLYD AYELKHALKG AGTDEKVLTE IIASRTPEEL 

       130        140        150        160        170        180 
SAIKQVYEEE YGSNLEDDVV GDTSGYYQRM LVVLLQANRD PDTAIDDAQV ELDAQALFQA 

       190        200        210        220        230        240 
GELKWGTDEE KFITIFGTRS VSHLRRVFDK YMTISGFQIE ETIDRETSGN LEQLLLAVVK 

       250        260        270        280        290        300 
SIRSIPAYLA ETLYYAMKGA GTDDHTLIRV VVSRSEIDLF NIRKEFRKNF ATSLYSMIKG 

       310 
DTSGDYKKAL LLLCGGEDD 

« Hide

References

« Hide 'large scale' references
[1]"Mouse annexin V chromosomal localization, cDNA sequence conservation, and molecular evolution."
Rodriguez-Garcia M.I., Kozak C.A., Morgan R.O., Fernandez M.-P.
Genomics 31:151-157(1996) [PubMed: 8824796] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Peritoneal cavity.
[2]Adachi T., Kojima K., Fukuoka S., Ogawa H., Matsumoto I.
Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Mouse annexin V genomic organization includes an endogenous retrovirus."
Rodriguez-Garcia M.I., Morgan R.O., Fernandez M.R., Bances P., Fernandez M.-P.
Biochem. J. 337:125-131(1999) [PubMed: 9854034] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 129/SvJ.
Tissue: Liver.
[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: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Bone marrow.
[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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Mammary gland.
[6]Lubec G., Klug S., Kang S.U.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 28-43; 62-74; 116-124; 192-199; 226-240 AND 275-283, MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain and Hippocampus.
+Additional computationally mapped references.

Cross-references

Sequence databases

U29396 mRNA. Translation: AAC52530.1.
D63423 mRNA. Translation: BAA09728.1.
AJ230108 expand/collapse EMBL AC list , AJ230110, AJ230111, AJ230114, AJ230116, AJ230118, AJ230119, AJ230120, AJ230121, AJ230122, AJ230123, AJ230124 Genomic DNA. Translation: CAA13092.1.
AK147740 mRNA. Translation: BAE28107.1.
AK152185 mRNA. Translation: BAE31016.1.
AK153388 mRNA. Translation: BAE31952.1.
AK153476 mRNA. Translation: BAE32026.1.
BC003716 mRNA. Translation: AAH03716.1.
IPIIPI00317309.
RefSeqNP_033803.1.
UniGeneMm.1620

3D structure databases

HSSPHSSP built from PDB template 1A8B based on UniProtKB P14668.
SMRP48036. Positions 2-319.
ModBaseSearch...

PTM databases

PhosphoSiteP48036.

2-D gel databases

SWISS-2DPAGEP48036.

Proteomic databases

PRIDEP48036.

Genome annotation databases

EnsemblENSMUSG00000027712. Mus musculus. [Contig view]
GeneID11747.
KEGGmmu:11747.
NMPDRfig|10090.3.peg.7935.

Organism-specific databases

MGIMGI:106008. Anxa5.

Phylogenomic databases

HOGENOMP48036.
HOVERGENP48036.
OMAP48036. SVSHLRR.

Gene expression databases

ArrayExpressP48036.
BgeeP48036.
CleanExMM_ANXA5.
GermOnlineENSMUSG00000027712. Mus musculus.

Family and domain databases

InterProIPR001464. Annexin.
IPR018502. Annexin_repeat.
IPR018252. Annexin_repeat_CS.
IPR015473. Annexins_V.
IPR002392. AnnexinV.
[Graphical view]
Gene3DG3DSA:1.10.220.10. Annexin. 4 hits.
PANTHERPTHR10502. Annexin. 1 hit.
PTHR10502:SF26. Annexins_V. 1 hit.
PfamPF00191. Annexin. 4 hits.
[Graphical view]
PRINTSPR00196. ANNEXIN.
PR00201. ANNEXINV.
ProDomPD000143. Annexin. 4 hits.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00335. ANX. 4 hits.
[Graphical view]
PROSITEPS00223. ANNEXIN. 4 hits.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio279485.
SOURCESearch...

Entry information

Entry nameANXA5_MOUSE
AccessionPrimary (citable) accession number: P48036
Secondary accession number(s): Q3U5Q1 expand/collapse secondary AC list , Q3U5X4, Q3U8K1, Q3UGV0, Q99LA1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: June 16, 2009
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents