ANXA9_MOUSE
ID ANXA9_MOUSE Reviewed; 345 AA.
AC Q9JHQ0; Q9CQS1;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Annexin A9;
DE AltName: Full=Annexin XXXI;
DE AltName: Full=Annexin-31;
DE AltName: Full=Annexin-9;
GN Name=Anxa9;
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 [GENOMIC DNA].
RC STRAIN=129/Sv;
RX DOI=10.1166/gl.2002.020;
RA Markoff A., Kuryshev V., Vorobyov E., Bogdanova N., Rescher U.,
RA Goebeler V., Kondrashov A., Gerke V.;
RT "Structure and expression of the murine annexin A9 gene.";
RL Genome Lett. 1:189-197(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Fernandez M.-P., Copeland N.G., Jenkins N.A., Gilbert D.J., Morgan R.O.;
RT "Role of ancient chromosomal duplications in the conserved gene
RT organization, paralogous linkage and RGD synaptomorphy of annexins A1, A2
RT and A9.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Tongue;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Jaw, and Limb;
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).
CC -!- FUNCTION: May act as a low affinity receptor for acetylcholine.
CC {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the annexin family. {ECO:0000255|PROSITE-
CC ProRule:PRU01245, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB95698.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF437742; AAO37381.1; -; Genomic_DNA.
DR EMBL; AJ401160; CAB95698.1; ALT_FRAME; mRNA.
DR EMBL; AK010128; BAB26719.1; -; mRNA.
DR EMBL; AK003395; BAB22761.1; -; mRNA.
DR EMBL; BC062140; AAH62140.1; -; mRNA.
DR CCDS; CCDS50989.1; -.
DR RefSeq; NP_001078852.1; NM_001085383.1.
DR RefSeq; NP_076117.2; NM_023628.2.
DR RefSeq; XP_011238537.1; XM_011240235.1.
DR AlphaFoldDB; Q9JHQ0; -.
DR SMR; Q9JHQ0; -.
DR STRING; 10090.ENSMUSP00000102801; -.
DR PhosphoSitePlus; Q9JHQ0; -.
DR MaxQB; Q9JHQ0; -.
DR PaxDb; Q9JHQ0; -.
DR PRIDE; Q9JHQ0; -.
DR ProteomicsDB; 281777; -.
DR Antibodypedia; 34042; 221 antibodies from 24 providers.
DR DNASU; 71790; -.
DR Ensembl; ENSMUST00000015846; ENSMUSP00000015846; ENSMUSG00000015702.
DR Ensembl; ENSMUST00000107183; ENSMUSP00000102801; ENSMUSG00000015702.
DR Ensembl; ENSMUST00000164406; ENSMUSP00000127424; ENSMUSG00000015702.
DR GeneID; 71790; -.
DR KEGG; mmu:71790; -.
DR UCSC; uc008qjg.1; mouse.
DR CTD; 8416; -.
DR MGI; MGI:1923711; Anxa9.
DR VEuPathDB; HostDB:ENSMUSG00000015702; -.
DR eggNOG; KOG0819; Eukaryota.
DR GeneTree; ENSGT00940000161835; -.
DR HOGENOM; CLU_025300_0_0_1; -.
DR InParanoid; Q9JHQ0; -.
DR OMA; HNFQVEA; -.
DR OrthoDB; 856254at2759; -.
DR PhylomeDB; Q9JHQ0; -.
DR TreeFam; TF105452; -.
DR BioGRID-ORCS; 71790; 1 hit in 77 CRISPR screens.
DR ChiTaRS; Anxa9; mouse.
DR PRO; PR:Q9JHQ0; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9JHQ0; protein.
DR Bgee; ENSMUSG00000015702; Expressed in esophagus and 100 other tissues.
DR ExpressionAtlas; Q9JHQ0; baseline and differential.
DR Genevisible; Q9JHQ0; MM.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0031982; C:vesicle; IBA:GO_Central.
DR GO; GO:0015464; F:acetylcholine receptor activity; ISS:UniProtKB.
DR GO; GO:0005262; F:calcium channel activity; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IBA:GO_Central.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IBA:GO_Central.
DR GO; GO:0001786; F:phosphatidylserine binding; ISS:UniProtKB.
DR GO; GO:0019834; F:phospholipase A2 inhibitor activity; IBA:GO_Central.
DR GO; GO:0005543; F:phospholipid binding; ISS:UniProtKB.
DR GO; GO:0002020; F:protease binding; IBA:GO_Central.
DR GO; GO:0046790; F:virion binding; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; ISS:UniProtKB.
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; IPR009116; ANX9.
DR PANTHER; PTHR10502:SF122; PTHR10502:SF122; 1.
DR Pfam; PF00191; Annexin; 4.
DR PRINTS; PR00196; ANNEXIN.
DR PRINTS; PR01812; ANNEXINXXXI.
DR SMART; SM00335; ANX; 4.
DR SUPFAM; SSF47874; SSF47874; 1.
DR PROSITE; PS00223; ANNEXIN_1; 1.
DR PROSITE; PS51897; ANNEXIN_2; 4.
PE 2: Evidence at transcript level;
KW Annexin; Reference proteome; Repeat.
FT CHAIN 1..345
FT /note="Annexin A9"
FT /id="PRO_0000067506"
FT REPEAT 41..112
FT /note="Annexin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 113..184
FT /note="Annexin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 197..266
FT /note="Annexin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 270..341
FT /note="Annexin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT CONFLICT 145..147
FT /note="APG -> FSR (in Ref. 2; CAB95698)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 345 AA; 38110 MW; 638EF32FFFFB6AF0 CRC64;
MSASCGPLGT SLTQEILSSL GLADKTAAWG TLGTLRTFLS FSVDKDVQRL LKAIAGQGVD
YDTIVDVLTN RSREQRQLIS RAFQERTKQD LLKSLQAALS GNLEKIVVAL LQPAAQFDAQ
ELRTALKTSG SAEDVALEIL ATRAAPGLQA CLAVYKHDFQ VEAEEDIRTE TNGILQDLLL
ALSKGDRESY SGIIDYNLEE QDVRALQQAG ESSTAGQWVL LLTQRSPEHL IRVFDQYRRC
TGQELEDAIR NCFHGDAQLA LISLASMLRN TALYFANKLH QALQETEPNF QVLTRVLISR
SESDLLSIRA EFKKKFGKSL YSSLQDVVRG DCRSALLALC RAEDI
