ANXA4_MOUSE
ID ANXA4_MOUSE Reviewed; 319 AA.
AC P97429; Q3UCL0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 4.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Annexin A4;
DE AltName: Full=Annexin IV;
DE AltName: Full=Annexin-4;
GN Name=Anxa4; Synonyms=Anx4;
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=C3H/HeJ;
RA Sable C.L., Shannon J., Riches D.W.H.;
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Bone marrow, Extraembryonic tissue, Heart, Kidney, Placenta, and
RC Stomach;
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 GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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).
CC -!- FUNCTION: Calcium/phospholipid-binding protein which promotes membrane
CC fusion and is involved in exocytosis. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Zymogen granule membrane
CC {ECO:0000250|UniProtKB:P50994}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P50994}.
CC -!- DOMAIN: A pair of annexin repeats may form one binding site for calcium
CC and phospholipid.
CC -!- MISCELLANEOUS: Seems to bind one calcium ion with high affinity.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the annexin family. {ECO:0000255|PROSITE-
CC ProRule:PRU01245, ECO:0000305}.
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DR EMBL; U72941; AAB40697.1; -; mRNA.
DR EMBL; AK132293; BAE21085.1; -; mRNA.
DR EMBL; AK150486; BAE29602.1; -; mRNA.
DR EMBL; AK150614; BAE29705.1; -; mRNA.
DR EMBL; AK151054; BAE30071.1; -; mRNA.
DR EMBL; AK151236; BAE30228.1; -; mRNA.
DR EMBL; AK167338; BAE39439.1; -; mRNA.
DR EMBL; AK168390; BAE40316.1; -; mRNA.
DR EMBL; AK168487; BAE40374.1; -; mRNA.
DR EMBL; AK168917; BAE40730.1; -; mRNA.
DR EMBL; AK170447; BAE41805.1; -; mRNA.
DR EMBL; CH466523; EDK99195.1; -; Genomic_DNA.
DR CCDS; CCDS39543.1; -.
DR RefSeq; NP_001318049.1; NM_001331120.1.
DR RefSeq; NP_038499.2; NM_013471.2.
DR RefSeq; XP_006505460.1; XM_006505397.2.
DR RefSeq; XP_006505461.1; XM_006505398.2.
DR AlphaFoldDB; P97429; -.
DR SMR; P97429; -.
DR BioGRID; 198110; 3.
DR IntAct; P97429; 6.
DR STRING; 10090.ENSMUSP00000109305; -.
DR iPTMnet; P97429; -.
DR PhosphoSitePlus; P97429; -.
DR SwissPalm; P97429; -.
DR EPD; P97429; -.
DR jPOST; P97429; -.
DR MaxQB; P97429; -.
DR PaxDb; P97429; -.
DR PeptideAtlas; P97429; -.
DR PRIDE; P97429; -.
DR ProteomicsDB; 281776; -.
DR Antibodypedia; 1552; 502 antibodies from 42 providers.
DR DNASU; 11746; -.
DR Ensembl; ENSMUST00000001187; ENSMUSP00000001187; ENSMUSG00000029994.
DR Ensembl; ENSMUST00000113675; ENSMUSP00000109305; ENSMUSG00000029994.
DR GeneID; 11746; -.
DR KEGG; mmu:11746; -.
DR UCSC; uc009csm.2; mouse.
DR CTD; 307; -.
DR MGI; MGI:88030; Anxa4.
DR VEuPathDB; HostDB:ENSMUSG00000029994; -.
DR eggNOG; KOG0819; Eukaryota.
DR GeneTree; ENSGT00940000156575; -.
DR HOGENOM; CLU_025300_0_0_1; -.
DR InParanoid; P97429; -.
DR OMA; RHFMIVL; -.
DR OrthoDB; 856254at2759; -.
DR PhylomeDB; P97429; -.
DR TreeFam; TF105452; -.
DR BioGRID-ORCS; 11746; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Anxa4; mouse.
DR PRO; PR:P97429; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; P97429; protein.
DR Bgee; ENSMUSG00000029994; Expressed in small intestine Peyer's patch and 234 other tissues.
DR ExpressionAtlas; P97429; baseline and differential.
DR Genevisible; P97429; MM.
DR GO; GO:0016324; C:apical plasma membrane; ISA:MGI.
DR GO; GO:0009986; C:cell surface; 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:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0012506; C:vesicle membrane; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; ISO:MGI.
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:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0051059; F:NF-kappaB binding; ISO:MGI.
DR GO; GO:0030855; P:epithelial cell differentiation; IEA:Ensembl.
DR GO; GO:0001822; P:kidney development; ISA:MGI.
DR GO; GO:0032717; P:negative regulation of interleukin-8 production; ISO:MGI.
DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; ISO:MGI.
DR GO; GO:0007219; P:Notch signaling pathway; IDA:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
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; IPR002391; ANX4.
DR PANTHER; PTHR10502:SF28; PTHR10502:SF28; 1.
DR Pfam; PF00191; Annexin; 4.
DR PRINTS; PR00196; ANNEXIN.
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 Cytoplasmic vesicle; Membrane; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..319
FT /note="Annexin A4"
FT /id="PRO_0000067483"
FT REPEAT 14..85
FT /note="Annexin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 86..157
FT /note="Annexin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 169..241
FT /note="Annexin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 245..316
FT /note="Annexin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT MOD_RES 7
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P08132"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09525"
FT MOD_RES 213
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09525"
FT MOD_RES 293
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09525"
FT MOD_RES 300
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09525"
FT CONFLICT 154
FT /note="S -> F (in Ref. 1; AAB40697)"
FT /evidence="ECO:0000305"
FT CONFLICT 313
FT /note="V -> I (in Ref. 1; AAB40697)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 319 AA; 35916 MW; D962B63D7933EBB9 CRC64;
MEAKGGTVKA ASGFNATEDA QTLRKAMKGL GTDEDAIIGI LAYRNTAQRQ EIRSAYKSTI
GRDLIEDLKS ELSSNFEQVI LGLMTPTVLY DVQELRRAMK GAGTDEGCLI EILASRTPEE
IRRINQTYQQ QYGRSLEEDI CSDTSFMFQR VLVSLSAAGR DEGNYLDDAL MKQDAQELYE
AGEKRWGTDE VKFLSILCSR NRNHLLHVFD EYKRISQKDI EQSIKSETSG SFEDALLAIV
KCMRSKPSYF AERLYKSMKG LGTDDNTLIR VMVSRAEIDM LDIRASFKRL YGKSLYSFIK
GDTSGDYRKV LLVLCGGDD
