ANXA3_RAT
ID ANXA3_RAT Reviewed; 324 AA.
AC P14669; Q642C2;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, 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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2968983; DOI=10.1016/s0021-9258(18)38041-4;
RA Pepinsky R.B., Tizard R., Mattaliano R.J., Sinclair L.K., Miller G.T.,
RA Browning J.L., Chow E.P., Burne C., Huang K.-S., Pratt D., Wachter L.,
RA Hession C., Frey A.Z., Wallner B.P.;
RT "Five distinct calcium and phospholipid binding proteins share homology
RT with lipocortin I.";
RL J. Biol. Chem. 263:10799-10811(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
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 [3]
RP PROTEIN SEQUENCE OF 41-49; 191-205; 231-246 AND 295-313, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-268, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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; M20559; AAA41511.1; -; mRNA.
DR EMBL; BC081856; AAH81856.1; -; mRNA.
DR PIR; A29250; LURT3.
DR RefSeq; NP_036955.2; NM_012823.2.
DR RefSeq; XP_006250756.1; XM_006250694.3.
DR RefSeq; XP_006250758.1; XM_006250696.3.
DR AlphaFoldDB; P14669; -.
DR SMR; P14669; -.
DR IntAct; P14669; 4.
DR STRING; 10116.ENSRNOP00000063496; -.
DR iPTMnet; P14669; -.
DR PhosphoSitePlus; P14669; -.
DR World-2DPAGE; 0004:P14669; -.
DR PaxDb; P14669; -.
DR PRIDE; P14669; -.
DR Ensembl; ENSRNOT00000068134; ENSRNOP00000063496; ENSRNOG00000002045.
DR GeneID; 25291; -.
DR KEGG; rno:25291; -.
DR UCSC; RGD:2119; rat.
DR CTD; 306; -.
DR RGD; 2119; Anxa3.
DR eggNOG; KOG0819; Eukaryota.
DR GeneTree; ENSGT00940000159174; -.
DR HOGENOM; CLU_025300_0_0_1; -.
DR InParanoid; P14669; -.
DR OMA; CKLWVGH; -.
DR OrthoDB; 856254at2759; -.
DR PhylomeDB; P14669; -.
DR PRO; PR:P14669; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Bgee; ENSRNOG00000002045; Expressed in lung and 20 other tissues.
DR ExpressionAtlas; P14669; baseline and differential.
DR Genevisible; P14669; RN.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0030670; C:phagocytic vesicle membrane; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0042581; C:specific granule; ISO:RGD.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IDA:RGD.
DR GO; GO:0048306; F:calcium-dependent protein binding; ISO:RGD.
DR GO; GO:0019834; F:phospholipase A2 inhibitor activity; IDA:RGD.
DR GO; GO:0031100; P:animal organ regeneration; IEP:RGD.
DR GO; GO:0042742; P:defense response to bacterium; ISO:RGD.
DR GO; GO:0021766; P:hippocampus development; IEP:RGD.
DR GO; GO:0043312; P:neutrophil degranulation; ISO:RGD.
DR GO; GO:0006909; P:phagocytosis; ISO:RGD.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISO:RGD.
DR GO; GO:0051054; P:positive regulation of DNA metabolic process; IMP:RGD.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISO:RGD.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; ISO:RGD.
DR GO; GO:0051384; P:response to glucocorticoid; IEP:RGD.
DR GO; GO:0070848; P:response to growth factor; IEP:RGD.
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 Direct protein sequencing; Phospholipase A2 inhibitor; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..324
FT /note="Annexin A3"
FT /id="PRO_0000067479"
FT REPEAT 19..90
FT /note="Annexin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 91..162
FT /note="Annexin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 174..246
FT /note="Annexin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 250..321
FT /note="Annexin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT MOD_RES 178
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O35639"
FT MOD_RES 268
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CONFLICT 60..61
FT /note="QY -> HI (in Ref. 1; AAA41511)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 324 AA; 36363 MW; AD10CBB301A01E41 CRC64;
MAASLWVGPR GTINNYPGFN PSVDAEAIRK AIKGIGTDEK TLINILTERS NAQRQLIVKQ
YQEAYEQALK ADLKGDLSGH FEHVMVALIT APAVFDAKQL KKSMRGMGTD EDTLIEILTT
RTSRQMKEIS QAYYTAYKKN LRDDISSETS GDFRKALLTL ADGGRDESLK VDEHLAKKDA
QTLYDAGEKK WGTDEDKFTE ILCLRSFPQL KLTFDEYRNI SQKDIEDSIK GELSGHFEDL
LLAVVRCTRN TPAFLAGRLH QALKGAGTDE FTLNRIMVSR SEIDLLDIRR EFKKHYGCSL
YSAIQSDTSG DYRTVLLKIC GGDD
