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O35639

- ANXA3_MOUSE

UniProt

O35639 - ANXA3_MOUSE

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Protein
Annexin A3
Gene
Anxa3, Anx3
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Inhibitor of phospholipase A2, also possesses anti-coagulant properties.

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. calcium-dependent phospholipid binding Source: UniProtKB-KW
  3. phospholipase A2 inhibitor activity Source: UniProtKB-KW
Complete GO annotation...

GO - Biological processi

  1. defense response to bacterium Source: Ensembl
  2. neutrophil degranulation Source: Ensembl
  3. phagocytosis Source: Ensembl
  4. positive regulation of angiogenesis Source: Ensembl
  5. positive regulation of endothelial cell migration Source: Ensembl
  6. positive regulation of sequence-specific DNA binding transcription factor activity Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Phospholipase A2 inhibitor

Keywords - Ligandi

Calcium, Calcium/phospholipid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Annexin A3
Alternative name(s):
35-alpha calcimedin
Annexin III
Annexin-3
Lipocortin III
Placental anticoagulant protein III
Short name:
PAP-III
Gene namesi
Name:Anxa3
Synonyms:Anx3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 5

Organism-specific databases

MGIiMGI:1201378. Anxa3.

Subcellular locationi

GO - Cellular componenti

  1. phagocytic vesicle membrane Source: Ensembl
  2. plasma membrane Source: Ensembl
  3. specific granule Source: Ensembl
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 323322Annexin A3
PRO_0000067478Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine By similarity
Modified residuei177 – 1771N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiO35639.
PaxDbiO35639.
PRIDEiO35639.

2D gel databases

COMPLUYEAST-2DPAGEO35639.
REPRODUCTION-2DPAGEO35639.

PTM databases

PhosphoSiteiO35639.

Expressioni

Gene expression databases

BgeeiO35639.
CleanExiMM_ANXA3.
GenevestigatoriO35639.

Interactioni

Protein-protein interaction databases

BioGridi198109. 1 interaction.
IntActiO35639. 3 interactions.
MINTiMINT-4996194.

Structurei

3D structure databases

ProteinModelPortaliO35639.
SMRiO35639. Positions 2-323.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati27 – 8761Annexin 1
Add
BLAST
Repeati99 – 15961Annexin 2
Add
BLAST
Repeati183 – 24361Annexin 3
Add
BLAST
Repeati258 – 31861Annexin 4
Add
BLAST

Domaini

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

Sequence similaritiesi

Belongs to the annexin family.
Contains 4 annexin repeats.

Keywords - Domaini

Annexin, Repeat

Phylogenomic databases

eggNOGiNOG267770.
GeneTreeiENSGT00740000115158.
HOGENOMiHOG000158803.
HOVERGENiHBG061815.
InParanoidiQ3UBI0.
KOiK17089.
OMAiHRGTVRD.
OrthoDBiEOG74XS72.
TreeFamiTF105452.

Family and domain databases

Gene3Di1.10.220.10. 4 hits.
InterProiIPR001464. Annexin.
IPR018502. Annexin_repeat.
IPR018252. Annexin_repeat_CS.
IPR002390. AnnexinIII.
[Graphical view]
PANTHERiPTHR10502:SF25. PTHR10502:SF25. 1 hit.
PfamiPF00191. Annexin. 4 hits.
[Graphical view]
PRINTSiPR00196. ANNEXIN.
PR00199. ANNEXINIII.
SMARTiSM00335. ANX. 4 hits.
[Graphical view]
PROSITEiPS00223. ANNEXIN. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O35639-1 [UniParc]FASTAAdd to Basket

« Hide

MASIWVGPRG TIKDYPGFSP SVDAEAIRKA IRGLGTDEKT LINILTERSN    50
AQRQLIVKQY QAAYEQELKD DLKGDLSGHF EHVMVALVTA PALFDAKQLK 100
KSMKGTGTDE DALIEILTTR SSRQMKEISQ AYYTVYKKSL GDDISSETSG 150
DFRKALLTLA DGRRDESLKV DEHLAKKDAQ ILYNAGENKW GTDEDKFTEV 200
LCLRSFPQLK LTFDEYRNIS QKDIEDSIKG ELSGHFEDLL LAIVHCARNT 250
PAFLAERLHQ ALKGAGTDEF TLNRIMVSRS EIDLLDIRHE FKKHYGYSLY 300
SAIQSDTSGD YRTVLLKICG EDD 323
Length:323
Mass (Da):36,384
Last modified:July 27, 2011 - v4
Checksum:iE869F181A8AC60B9
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti97 – 982KQ → NE in CAA04887. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ001633 mRNA. Translation: CAA04887.1.
AK150922 mRNA. Translation: BAE29960.1.
AK150951 mRNA. Translation: BAE29984.1.
AK151771 mRNA. Translation: BAE30677.1.
AK152863 mRNA. Translation: BAE31554.1.
AK168396 mRNA. Translation: BAE40320.1.
AK168507 mRNA. Translation: BAE40390.1.
BC090634 mRNA. Translation: AAH90634.1.
CCDSiCCDS51568.1.
RefSeqiNP_038498.2. NM_013470.2.
XP_006534797.1. XM_006534734.1.
UniGeneiMm.7214.

Genome annotation databases

EnsembliENSMUST00000031447; ENSMUSP00000031447; ENSMUSG00000029484.
GeneIDi11745.
KEGGimmu:11745.
UCSCiuc008yfm.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ001633 mRNA. Translation: CAA04887.1 .
AK150922 mRNA. Translation: BAE29960.1 .
AK150951 mRNA. Translation: BAE29984.1 .
AK151771 mRNA. Translation: BAE30677.1 .
AK152863 mRNA. Translation: BAE31554.1 .
AK168396 mRNA. Translation: BAE40320.1 .
AK168507 mRNA. Translation: BAE40390.1 .
BC090634 mRNA. Translation: AAH90634.1 .
CCDSi CCDS51568.1.
RefSeqi NP_038498.2. NM_013470.2.
XP_006534797.1. XM_006534734.1.
UniGenei Mm.7214.

3D structure databases

ProteinModelPortali O35639.
SMRi O35639. Positions 2-323.
ModBasei Search...

Protein-protein interaction databases

BioGridi 198109. 1 interaction.
IntActi O35639. 3 interactions.
MINTi MINT-4996194.

PTM databases

PhosphoSitei O35639.

2D gel databases

COMPLUYEAST-2DPAGE O35639.
REPRODUCTION-2DPAGE O35639.

Proteomic databases

MaxQBi O35639.
PaxDbi O35639.
PRIDEi O35639.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000031447 ; ENSMUSP00000031447 ; ENSMUSG00000029484 .
GeneIDi 11745.
KEGGi mmu:11745.
UCSCi uc008yfm.2. mouse.

Organism-specific databases

CTDi 306.
MGIi MGI:1201378. Anxa3.

Phylogenomic databases

eggNOGi NOG267770.
GeneTreei ENSGT00740000115158.
HOGENOMi HOG000158803.
HOVERGENi HBG061815.
InParanoidi Q3UBI0.
KOi K17089.
OMAi HRGTVRD.
OrthoDBi EOG74XS72.
TreeFami TF105452.

Miscellaneous databases

NextBioi 279477.
PROi O35639.
SOURCEi Search...

Gene expression databases

Bgeei O35639.
CleanExi MM_ANXA3.
Genevestigatori O35639.

Family and domain databases

Gene3Di 1.10.220.10. 4 hits.
InterProi IPR001464. Annexin.
IPR018502. Annexin_repeat.
IPR018252. Annexin_repeat_CS.
IPR002390. AnnexinIII.
[Graphical view ]
PANTHERi PTHR10502:SF25. PTHR10502:SF25. 1 hit.
Pfami PF00191. Annexin. 4 hits.
[Graphical view ]
PRINTSi PR00196. ANNEXIN.
PR00199. ANNEXINIII.
SMARTi SM00335. ANX. 4 hits.
[Graphical view ]
PROSITEi PS00223. ANNEXIN. 4 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Mouse annexin III cDNA, genetic mapping and evolution."
    Fernandez M.-P., Copeland N.G., Gilbert D.J., Jenkins N.A., Morgan R.O.
    Gene 207:43-51(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6J.
  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.
    , 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: Amnion, Bone marrow and Liver.
  3. "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: C57BL/6.
    Tissue: Eye.
  4. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-177, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiANXA3_MOUSE
AccessioniPrimary (citable) accession number: O35639
Secondary accession number(s): Q3UBI0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 110 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi