ID   ANX11_MOUSE             Reviewed;         503 AA.
AC   P97384; Q921F1;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   02-SEP-2026, entry version 179.
DE   RecName: Full=Annexin A11;
DE   AltName: Full=Annexin XI;
DE   AltName: Full=Annexin-11;
DE   AltName: Full=Calcyclin-associated annexin 50;
DE            Short=CAP-50;
GN   Name=Anxa11; Synonyms=Anx11;
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].
RX   PubMed=8938449; DOI=10.1006/geno.1996.0571;
RA   Fernandez M.-P., Jenkins N.A., Gilbert D.J., Copeland N.G., Morgan R.O.;
RT   "Sequence and chromosomal localization of mouse annexin XI.";
RL   Genomics 37:366-374(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/SvJ;
RX   PubMed=11013079; DOI=10.1006/geno.2000.6309;
RA   Bances P., Fernandez M.R., Rodriguez-Garcia M.I., Morgan R.O.,
RA   Fernandez M.-P.;
RT   "Annexin A11 (ANXA11) gene structure as the progenitor of paralogous
RT   annexins and source of orthologous cDNA isoforms.";
RL   Genomics 69:95-103(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain cortex;
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].
RA   Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J.,
RA   Wiemann S., Schick M., Korn B.;
RT   "Cloning of mouse full open reading frames in Gateway(R) system entry
RT   vector (pDONR201).";
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
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   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, 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: Required for midbody formation and completion of the terminal
CC       phase of cytokinesis (By similarity). Binds specifically to calcyclin
CC       in a calcium-dependent manner. {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with S100A6. Interacts with PDCD6 in a calcium-
CC       dependent manner. Interacts with KIF23 during cytokinesis.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Melanosome
CC       {ECO:0000250}. Nucleus envelope {ECO:0000250}. Nucleus, nucleoplasm
CC       {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}.
CC       Note=Found throughout the nucleoplasm at interphase and during mitosis
CC       concentrates around the mitotic apparatus. Elevation of intracellular
CC       calcium causes relocalization from the nucleoplasm to the nuclear
CC       envelope, with little effect on the cytoplasmic pool. Localization to
CC       the nuclear envelope is cell-cycle dependent. {ECO:0000250}.
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; U65986; AAB42012.1; -; mRNA.
DR   EMBL; AJ289760; CAB94770.1; -; Genomic_DNA.
DR   EMBL; AJ289761; CAB94770.1; JOINED; Genomic_DNA.
DR   EMBL; AJ289762; CAB94770.1; JOINED; Genomic_DNA.
DR   EMBL; AJ289763; CAB94770.1; JOINED; Genomic_DNA.
DR   EMBL; AJ289764; CAB94770.1; JOINED; Genomic_DNA.
DR   EMBL; AJ289765; CAB94770.1; JOINED; Genomic_DNA.
DR   EMBL; AJ289766; CAB94770.1; JOINED; Genomic_DNA.
DR   EMBL; AJ289767; CAB94770.1; JOINED; Genomic_DNA.
DR   EMBL; AJ289768; CAB94770.1; JOINED; Genomic_DNA.
DR   EMBL; AJ289769; CAB94770.1; JOINED; Genomic_DNA.
DR   EMBL; AK140375; BAE24363.1; -; mRNA.
DR   EMBL; CT010331; CAJ18539.1; -; mRNA.
DR   EMBL; CH466613; EDL01415.1; -; Genomic_DNA.
DR   EMBL; BC012875; AAH12875.1; -; mRNA.
DR   CCDS; CCDS26875.1; -.
DR   RefSeq; NP_038497.2; NM_013469.2.
DR   RefSeq; XP_006518514.1; XM_006518451.5.
DR   AlphaFoldDB; P97384; -.
DR   SMR; P97384; -.
DR   BioGRID; 198108; 5.
DR   FunCoup; P97384; 1677.
DR   STRING; 10090.ENSMUSP00000022416; -.
DR   GlyGen; P97384; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P97384; -.
DR   PhosphoSitePlus; P97384; -.
DR   SwissPalm; P97384; -.
DR   jPOST; P97384; -.
DR   PaxDb; 10090-ENSMUSP00000022416; -.
DR   PeptideAtlas; P97384; -.
DR   ProteomicsDB; 282126; -.
DR   Antibodypedia; 3904; 339 antibodies from 41 providers.
DR   DNASU; 11744; -.
DR   Ensembl; ENSMUST00000022416.15; ENSMUSP00000022416.8; ENSMUSG00000021866.16.
DR   GeneID; 11744; -.
DR   KEGG; mmu:11744; -.
DR   UCSC; uc007srv.2; mouse.
DR   AGR; MGI:108481; -.
DR   CTD; 311; -.
DR   MGI; MGI:108481; Anxa11.
DR   VEuPathDB; HostDB:ENSMUSG00000021866; -.
DR   eggNOG; KOG0819; Eukaryota.
DR   GeneTree; ENSGT00940000156914; -.
DR   HOGENOM; CLU_025300_6_0_1; -.
DR   InParanoid; P97384; -.
DR   OMA; GQQPMTY; -.
DR   OrthoDB; 37886at2759; -.
DR   PhylomeDB; P97384; -.
DR   BioGRID-ORCS; 11744; 1 hit in 79 CRISPR screens.
DR   PRO; PR:P97384; -.
DR   Proteomes; UP000000589; Chromosome 14.
DR   RNAct; P97384; protein.
DR   Bgee; ENSMUSG00000021866; Expressed in granulocyte and 113 other cell types or tissues.
DR   ExpressionAtlas; P97384; baseline and differential.
DR   GO; GO:0042582; C:azurophil granule; ISO:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005829; C:cytosol; ISO:GO_Central.
DR   GO; GO:0031012; C:extracellular matrix; HDA:BHF-UCL.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR   GO; GO:0005635; C:nuclear envelope; ISO:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; ISO:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0045335; C:phagocytic vesicle; ISO:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0042581; C:specific granule; ISO:GO_Central.
DR   GO; GO:0005819; C:spindle; ISS:UniProtKB.
DR   GO; GO:0012506; C:vesicle membrane; IBA:GO_Central.
DR   GO; GO:0005509; F:calcium ion binding; IDA:MGI.
DR   GO; GO:0005544; F:calcium-dependent phospholipid binding; IDA:MGI.
DR   GO; GO:0048306; F:calcium-dependent protein binding; ISO:GO_Central.
DR   GO; GO:0008429; F:phosphatidylethanolamine binding; IDA:MGI.
DR   GO; GO:0001786; F:phosphatidylserine binding; IBA:GO_Central.
DR   GO; GO:0044548; F:S100 protein binding; ISS:UniProtKB.
DR   GO; GO:0032506; P:cytokinetic process; ISS:UniProtKB.
DR   GO; GO:0006909; P:phagocytosis; IBA:GO_Central.
DR   GO; GO:0051592; P:response to calcium ion; ISO:GO_Central.
DR   FunFam; 1.10.220.10:FF:000001; Annexin; 1.
DR   FunFam; 1.10.220.10:FF:000002; Annexin; 1.
DR   FunFam; 1.10.220.10:FF:000003; Annexin; 1.
DR   FunFam; 1.10.220.10:FF:000004; Annexin; 1.
DR   Gene3D; 1.10.220.10; Annexin; 4.
DR   InterPro; IPR001464; Annexin.
DR   InterPro; IPR018502; Annexin_repeat.
DR   InterPro; IPR018252; Annexin_repeat_CS.
DR   InterPro; IPR037104; Annexin_sf.
DR   InterPro; IPR008157; ANX11.
DR   PANTHER; PTHR10502; ANNEXIN; 1.
DR   PANTHER; PTHR10502:SF29; ANNEXIN A11; 1.
DR   Pfam; PF00191; Annexin; 4.
DR   PRINTS; PR00196; ANNEXIN.
DR   PRINTS; PR01810; ANNEXINXI.
DR   SMART; SM00335; ANX; 4.
DR   SUPFAM; SSF47874; Annexin; 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; Cell cycle;
KW   Cell division; Cytoplasm; Cytoskeleton; Nucleus; Reference proteome;
KW   Repeat.
FT   CHAIN           1..503
FT                   /note="Annexin A11"
FT                   /id="PRO_0000067511"
FT   REPEAT          198..269
FT                   /note="Annexin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT   REPEAT          270..341
FT                   /note="Annexin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT   REPEAT          353..425
FT                   /note="Annexin 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT   REPEAT          429..500
FT                   /note="Annexin 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT   REGION          80..172
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        80..117
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        123..167
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         246
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P50995"
FT   MOD_RES         253
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P50995"
FT   MOD_RES         477
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P50995"
FT   CONFLICT        69
FT                   /note="V -> M (in Ref. 1; AAB42012 and 2; CAB94770)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   503 AA;  54079 MW;  33F3471EE21A0D32 CRC64;
     MSYPGYPPPA GGYPPAAPGG GPWGGAGYPP PSMPPIGLDN VANYAGQFNQ DYLSGMAANM
     SGTFGGANVP NLYPGAPGGG YPPVPPGGFG QPPPAQQPVP PYGMYPPPGG NPPPGMPSYP
     AYPGAPVPGQ PMPPTGQQPP GAYPGQPPMT YPGQSPMPPP GQQPVPSYPG YSGSSTITPA
     VPPAQFGNRG TITAASGFDP LRDAEVLRKA MKGFGTDEQA IIDCLGSRSN KQRQQILLSF
     KTAYGKDLIK DLKSELSGNF EKTILALMKT PVLFDVYEIK EAIKGAGTDE ACLIEIFASR
     SNEHIRELSR AYKTEFQKTL EEAIRSDTSG HFQRLLISLS QGNRDESTNV DMSLVQRDVQ
     ELYAAGENRL GTDESKFNAI LCSRSRAHLV AVFNEYQRMT GRDIEKSICR EMSGDLEQGM
     LAVVKCLKNT PAFFAERLNK AMRGAGTKDR TLIRIMVSRS ELDLLDIRAE YKRMYGKSLY
     HDITGDTSGD YRKILLKICG GND
//