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O35639

- ANXA3_MOUSE

UniProt

O35639 - ANXA3_MOUSE

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Protein

Annexin A3

Gene

Anxa3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

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

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. extracellular vesicular exosome Source: Ensembl
  2. phagocytic vesicle membrane Source: Ensembl
  3. plasma membrane Source: Ensembl
  4. specific granule Source: Ensembl
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 323322Annexin A3PRO_0000067478Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy 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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

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

Domaini

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

Sequence similaritiesi

Belongs to the annexin family.Curated
Contains 4 annexin repeats.Curated

Keywords - Domaini

Annexin, Repeat

Phylogenomic databases

eggNOGiNOG267770.
GeneTreeiENSGT00760000118972.
HOGENOMiHOG000158803.
HOVERGENiHBG061815.
InParanoidiO35639.
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

        10         20         30         40         50
MASIWVGPRG TIKDYPGFSP SVDAEAIRKA IRGLGTDEKT LINILTERSN
60 70 80 90 100
AQRQLIVKQY QAAYEQELKD DLKGDLSGHF EHVMVALVTA PALFDAKQLK
110 120 130 140 150
KSMKGTGTDE DALIEILTTR SSRQMKEISQ AYYTVYKKSL GDDISSETSG
160 170 180 190 200
DFRKALLTLA DGRRDESLKV DEHLAKKDAQ ILYNAGENKW GTDEDKFTEV
210 220 230 240 250
LCLRSFPQLK LTFDEYRNIS QKDIEDSIKG ELSGHFEDLL LAIVHCARNT
260 270 280 290 300
PAFLAERLHQ ALKGAGTDEF TLNRIMVSRS EIDLLDIRHE FKKHYGYSLY
310 320
SAIQSDTSGD YRTVLLKICG EDD
Length:323
Mass (Da):36,384
Last modified:July 27, 2011 - v4
Checksum:iE869F181A8AC60B9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti97 – 982KQ → NE in CAA04887. (PubMed:9511742)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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...
MobiDBi 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 ENSGT00760000118972.
HOGENOMi HOG000158803.
HOVERGENi HBG061815.
InParanoidi O35639.
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: October 29, 2014
This is version 112 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