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Protein

Annexin A4

Gene

Anxa4

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

Functioni

Calcium/phospholipid-binding protein which promotes membrane fusion and is involved in exocytosis.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Calcium, Calcium/phospholipid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Annexin A4
Alternative name(s):
Annexin IV
Annexin-4
Gene namesi
Name:Anxa4
Synonyms:Anx4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:88030. Anxa4.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 319318Annexin A4PRO_0000067483Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei7 – 71PhosphothreonineBy similarity
Modified residuei12 – 121PhosphoserineBy similarity
Modified residuei213 – 2131N6-acetyllysineBy similarity
Modified residuei293 – 2931N6-acetyllysineBy similarity
Modified residuei300 – 3001N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP97429.
MaxQBiP97429.
PaxDbiP97429.
PRIDEiP97429.

PTM databases

iPTMnetiP97429.
PhosphoSiteiP97429.
SwissPalmiP97429.

Expressioni

Gene expression databases

BgeeiP97429.
CleanExiMM_ANXA4.
ExpressionAtlasiP97429. baseline and differential.
GenevisibleiP97429. MM.

Interactioni

GO - Molecular functioni

Protein-protein interaction databases

IntActiP97429. 10 interactions.
MINTiMINT-4087883.
STRINGi10090.ENSMUSP00000001187.

Structurei

3D structure databases

ProteinModelPortaliP97429.
SMRiP97429. Positions 4-318.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati23 – 8361Annexin 1Add
BLAST
Repeati95 – 15561Annexin 2Add
BLAST
Repeati179 – 23961Annexin 3Add
BLAST
Repeati254 – 31461Annexin 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

eggNOGiKOG0819. Eukaryota.
ENOG410XPUN. LUCA.
GeneTreeiENSGT00760000118972.
HOGENOMiHOG000158803.
HOVERGENiHBG061815.
InParanoidiP97429.
KOiK17093.
OMAiGMMMPTV.
OrthoDBiEOG74XS72.
TreeFamiTF105452.

Family and domain databases

Gene3Di1.10.220.10. 4 hits.
InterProiIPR001464. Annexin.
IPR018502. Annexin_repeat.
IPR018252. Annexin_repeat_CS.
IPR002391. AnnexinIV.
[Graphical view]
PANTHERiPTHR10502:SF28. PTHR10502:SF28. 1 hit.
PfamiPF00191. Annexin. 4 hits.
[Graphical view]
PRINTSiPR00196. ANNEXIN.
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.

P97429-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEAKGGTVKA ASGFNATEDA QTLRKAMKGL GTDEDAIIGI LAYRNTAQRQ
60 70 80 90 100
EIRSAYKSTI GRDLIEDLKS ELSSNFEQVI LGLMTPTVLY DVQELRRAMK
110 120 130 140 150
GAGTDEGCLI EILASRTPEE IRRINQTYQQ QYGRSLEEDI CSDTSFMFQR
160 170 180 190 200
VLVSLSAAGR DEGNYLDDAL MKQDAQELYE AGEKRWGTDE VKFLSILCSR
210 220 230 240 250
NRNHLLHVFD EYKRISQKDI EQSIKSETSG SFEDALLAIV KCMRSKPSYF
260 270 280 290 300
AERLYKSMKG LGTDDNTLIR VMVSRAEIDM LDIRASFKRL YGKSLYSFIK
310
GDTSGDYRKV LLVLCGGDD
Length:319
Mass (Da):35,916
Last modified:July 27, 2011 - v4
Checksum:iD962B63D7933EBB9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti154 – 1541S → F in AAB40697 (Ref. 1) Curated
Sequence conflicti313 – 3131V → I in AAB40697 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U72941 mRNA. Translation: AAB40697.1.
AK132293 mRNA. Translation: BAE21085.1.
AK150486 mRNA. Translation: BAE29602.1.
AK150614 mRNA. Translation: BAE29705.1.
AK151054 mRNA. Translation: BAE30071.1.
AK151236 mRNA. Translation: BAE30228.1.
AK167338 mRNA. Translation: BAE39439.1.
AK168390 mRNA. Translation: BAE40316.1.
AK168487 mRNA. Translation: BAE40374.1.
AK168917 mRNA. Translation: BAE40730.1.
AK170447 mRNA. Translation: BAE41805.1.
CH466523 Genomic DNA. Translation: EDK99195.1.
CCDSiCCDS39543.1.
RefSeqiNP_038499.2. NM_013471.2.
XP_006505460.1. XM_006505397.2.
XP_006505461.1. XM_006505398.2.
XP_011239458.1. XM_011241156.1.
XP_011239459.1. XM_011241157.1.
UniGeneiMm.259702.

Genome annotation databases

EnsembliENSMUST00000001187; ENSMUSP00000001187; ENSMUSG00000029994.
ENSMUST00000113675; ENSMUSP00000109305; ENSMUSG00000029994.
GeneIDi11746.
KEGGimmu:11746.
UCSCiuc009csm.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U72941 mRNA. Translation: AAB40697.1.
AK132293 mRNA. Translation: BAE21085.1.
AK150486 mRNA. Translation: BAE29602.1.
AK150614 mRNA. Translation: BAE29705.1.
AK151054 mRNA. Translation: BAE30071.1.
AK151236 mRNA. Translation: BAE30228.1.
AK167338 mRNA. Translation: BAE39439.1.
AK168390 mRNA. Translation: BAE40316.1.
AK168487 mRNA. Translation: BAE40374.1.
AK168917 mRNA. Translation: BAE40730.1.
AK170447 mRNA. Translation: BAE41805.1.
CH466523 Genomic DNA. Translation: EDK99195.1.
CCDSiCCDS39543.1.
RefSeqiNP_038499.2. NM_013471.2.
XP_006505460.1. XM_006505397.2.
XP_006505461.1. XM_006505398.2.
XP_011239458.1. XM_011241156.1.
XP_011239459.1. XM_011241157.1.
UniGeneiMm.259702.

3D structure databases

ProteinModelPortaliP97429.
SMRiP97429. Positions 4-318.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP97429. 10 interactions.
MINTiMINT-4087883.
STRINGi10090.ENSMUSP00000001187.

PTM databases

iPTMnetiP97429.
PhosphoSiteiP97429.
SwissPalmiP97429.

Proteomic databases

EPDiP97429.
MaxQBiP97429.
PaxDbiP97429.
PRIDEiP97429.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000001187; ENSMUSP00000001187; ENSMUSG00000029994.
ENSMUST00000113675; ENSMUSP00000109305; ENSMUSG00000029994.
GeneIDi11746.
KEGGimmu:11746.
UCSCiuc009csm.2. mouse.

Organism-specific databases

CTDi307.
MGIiMGI:88030. Anxa4.

Phylogenomic databases

eggNOGiKOG0819. Eukaryota.
ENOG410XPUN. LUCA.
GeneTreeiENSGT00760000118972.
HOGENOMiHOG000158803.
HOVERGENiHBG061815.
InParanoidiP97429.
KOiK17093.
OMAiGMMMPTV.
OrthoDBiEOG74XS72.
TreeFamiTF105452.

Miscellaneous databases

PROiP97429.
SOURCEiSearch...

Gene expression databases

BgeeiP97429.
CleanExiMM_ANXA4.
ExpressionAtlasiP97429. baseline and differential.
GenevisibleiP97429. MM.

Family and domain databases

Gene3Di1.10.220.10. 4 hits.
InterProiIPR001464. Annexin.
IPR018502. Annexin_repeat.
IPR018252. Annexin_repeat_CS.
IPR002391. AnnexinIV.
[Graphical view]
PANTHERiPTHR10502:SF28. PTHR10502:SF28. 1 hit.
PfamiPF00191. Annexin. 4 hits.
[Graphical view]
PRINTSiPR00196. ANNEXIN.
SMARTiSM00335. ANX. 4 hits.
[Graphical view]
PROSITEiPS00223. ANNEXIN. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Sable C.L., Shannon J., Riches D.W.H.
    Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C3H/HeJ.
  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 and NOD.
    Tissue: Bone marrow, Extraembryonic tissue, Heart, Kidney, Placenta and Stomach.
  3. 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].
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiANXA4_MOUSE
AccessioniPrimary (citable) accession number: P97429
Secondary accession number(s): Q3UCL0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 27, 2011
Last modified: June 8, 2016
This is version 115 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Seems to bind one calcium ion with high affinity.By similarity

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.