ANXA3_MOUSE
ID ANXA3_MOUSE Reviewed; 323 AA.
AC O35639; Q3UBI0;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 4.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Annexin A3;
DE AltName: Full=35-alpha calcimedin;
DE AltName: Full=Annexin III;
DE AltName: Full=Annexin-3;
DE AltName: Full=Lipocortin III;
DE AltName: Full=Placental anticoagulant protein III;
DE Short=PAP-III;
GN Name=Anxa3; Synonyms=Anx3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=9511742; DOI=10.1016/s0378-1119(97)00602-1;
RA Fernandez M.-P., Copeland N.G., Gilbert D.J., Jenkins N.A., Morgan R.O.;
RT "Mouse annexin III cDNA, genetic mapping and evolution.";
RL Gene 207:43-51(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Amnion, Bone marrow, and Liver;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-177, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Inhibitor of phospholipase A2, also possesses anti-coagulant
CC properties.
CC -!- DOMAIN: A pair of annexin repeats may form one binding site for calcium
CC and phospholipid.
CC -!- SIMILARITY: Belongs to the annexin family. {ECO:0000255|PROSITE-
CC ProRule:PRU01245, ECO:0000305}.
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DR EMBL; AJ001633; CAA04887.1; -; mRNA.
DR EMBL; AK150922; BAE29960.1; -; mRNA.
DR EMBL; AK150951; BAE29984.1; -; mRNA.
DR EMBL; AK151771; BAE30677.1; -; mRNA.
DR EMBL; AK152863; BAE31554.1; -; mRNA.
DR EMBL; AK168396; BAE40320.1; -; mRNA.
DR EMBL; AK168507; BAE40390.1; -; mRNA.
DR EMBL; BC090634; AAH90634.1; -; mRNA.
DR CCDS; CCDS51568.1; -.
DR RefSeq; NP_038498.2; NM_013470.2.
DR AlphaFoldDB; O35639; -.
DR SMR; O35639; -.
DR BioGRID; 198109; 3.
DR IntAct; O35639; 1.
DR STRING; 10090.ENSMUSP00000031447; -.
DR iPTMnet; O35639; -.
DR PhosphoSitePlus; O35639; -.
DR COMPLUYEAST-2DPAGE; O35639; -.
DR REPRODUCTION-2DPAGE; O35639; -.
DR EPD; O35639; -.
DR jPOST; O35639; -.
DR MaxQB; O35639; -.
DR PaxDb; O35639; -.
DR PeptideAtlas; O35639; -.
DR PRIDE; O35639; -.
DR ProteomicsDB; 281775; -.
DR Antibodypedia; 2890; 624 antibodies from 35 providers.
DR DNASU; 11745; -.
DR Ensembl; ENSMUST00000031447; ENSMUSP00000031447; ENSMUSG00000029484.
DR GeneID; 11745; -.
DR KEGG; mmu:11745; -.
DR UCSC; uc008yfm.2; mouse.
DR CTD; 306; -.
DR MGI; MGI:1201378; Anxa3.
DR VEuPathDB; HostDB:ENSMUSG00000029484; -.
DR eggNOG; KOG0819; Eukaryota.
DR GeneTree; ENSGT00940000159174; -.
DR HOGENOM; CLU_025300_0_0_1; -.
DR InParanoid; O35639; -.
DR OMA; CKLWVGH; -.
DR OrthoDB; 856254at2759; -.
DR PhylomeDB; O35639; -.
DR TreeFam; TF105452; -.
DR BioGRID-ORCS; 11745; 2 hits in 76 CRISPR screens.
DR ChiTaRS; Anxa3; mouse.
DR PRO; PR:O35639; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; O35639; protein.
DR Bgee; ENSMUSG00000029484; Expressed in right lung lobe and 251 other tissues.
DR ExpressionAtlas; O35639; baseline and differential.
DR Genevisible; O35639; MM.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0030670; C:phagocytic vesicle membrane; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0042581; C:specific granule; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; ISO:MGI.
DR GO; GO:0048306; F:calcium-dependent protein binding; ISO:MGI.
DR GO; GO:0019834; F:phospholipase A2 inhibitor activity; ISO:MGI.
DR GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl.
DR GO; GO:0042742; P:defense response to bacterium; ISO:MGI.
DR GO; GO:0021766; P:hippocampus development; IEA:Ensembl.
DR GO; GO:0043312; P:neutrophil degranulation; ISO:MGI.
DR GO; GO:0006909; P:phagocytosis; ISO:MGI.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISO:MGI.
DR GO; GO:0051054; P:positive regulation of DNA metabolic process; ISO:MGI.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISO:MGI.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; ISO:MGI.
DR GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
DR GO; GO:0070848; P:response to growth factor; IEA:Ensembl.
DR Gene3D; 1.10.220.10; -; 4.
DR InterPro; IPR001464; Annexin.
DR InterPro; IPR018502; Annexin_repeat.
DR InterPro; IPR018252; Annexin_repeat_CS.
DR InterPro; IPR037104; Annexin_sf.
DR InterPro; IPR002390; ANX3.
DR PANTHER; PTHR10502:SF25; PTHR10502:SF25; 1.
DR Pfam; PF00191; Annexin; 4.
DR PRINTS; PR00196; ANNEXIN.
DR PRINTS; PR00199; ANNEXINIII.
DR SMART; SM00335; ANX; 4.
DR SUPFAM; SSF47874; SSF47874; 1.
DR PROSITE; PS00223; ANNEXIN_1; 4.
DR PROSITE; PS51897; ANNEXIN_2; 4.
PE 1: Evidence at protein level;
KW Acetylation; Annexin; Calcium; Calcium/phospholipid-binding;
KW Phospholipase A2 inhibitor; Phosphoprotein; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P12429"
FT CHAIN 2..323
FT /note="Annexin A3"
FT /id="PRO_0000067478"
FT REPEAT 18..89
FT /note="Annexin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 90..161
FT /note="Annexin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 173..245
FT /note="Annexin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 249..320
FT /note="Annexin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P12429"
FT MOD_RES 177
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 267
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P14669"
FT CONFLICT 97..98
FT /note="KQ -> NE (in Ref. 1; CAA04887)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 323 AA; 36384 MW; E869F181A8AC60B9 CRC64;
MASIWVGPRG TIKDYPGFSP SVDAEAIRKA IRGLGTDEKT LINILTERSN AQRQLIVKQY
QAAYEQELKD DLKGDLSGHF EHVMVALVTA PALFDAKQLK KSMKGTGTDE DALIEILTTR
SSRQMKEISQ AYYTVYKKSL GDDISSETSG DFRKALLTLA DGRRDESLKV DEHLAKKDAQ
ILYNAGENKW GTDEDKFTEV LCLRSFPQLK LTFDEYRNIS QKDIEDSIKG ELSGHFEDLL
LAIVHCARNT PAFLAERLHQ ALKGAGTDEF TLNRIMVSRS EIDLLDIRHE FKKHYGYSLY
SAIQSDTSGD YRTVLLKICG EDD
