ANX11_MOUSE
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 03-AUG-2022, entry version 161.
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, 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: 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_006518451.3.
DR AlphaFoldDB; P97384; -.
DR SMR; P97384; -.
DR BioGRID; 198108; 4.
DR STRING; 10090.ENSMUSP00000022416; -.
DR iPTMnet; P97384; -.
DR PhosphoSitePlus; P97384; -.
DR SwissPalm; P97384; -.
DR SWISS-2DPAGE; P97384; -.
DR EPD; P97384; -.
DR jPOST; P97384; -.
DR MaxQB; P97384; -.
DR PaxDb; P97384; -.
DR PeptideAtlas; P97384; -.
DR PRIDE; P97384; -.
DR ProteomicsDB; 282126; -.
DR Antibodypedia; 3904; 320 antibodies from 40 providers.
DR DNASU; 11744; -.
DR Ensembl; ENSMUST00000022416; ENSMUSP00000022416; ENSMUSG00000021866.
DR GeneID; 11744; -.
DR KEGG; mmu:11744; -.
DR UCSC; uc007srv.2; mouse.
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; MTYPGQQ; -.
DR OrthoDB; 856254at2759; -.
DR PhylomeDB; P97384; -.
DR TreeFam; TF105452; -.
DR BioGRID-ORCS; 11744; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Anxa11; mouse.
DR PRO; PR:P97384; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; P97384; protein.
DR Bgee; ENSMUSG00000021866; Expressed in granulocyte and 110 other tissues.
DR ExpressionAtlas; P97384; baseline and differential.
DR Genevisible; P97384; MM.
DR GO; GO:0042582; C:azurophil granule; ISO:MGI.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
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:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0045335; C:phagocytic vesicle; ISO:MGI.
DR GO; GO:0042581; C:specific granule; ISO:MGI.
DR GO; GO:0005819; C:spindle; ISS:UniProtKB.
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:MGI.
DR GO; GO:0008429; F:phosphatidylethanolamine binding; IDA:MGI.
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: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; IPR008157; ANX11.
DR PANTHER; PTHR10502:SF29; PTHR10502:SF29; 1.
DR Pfam; PF00191; Annexin; 4.
DR PRINTS; PR00196; ANNEXIN.
DR PRINTS; PR01810; ANNEXINXI.
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; 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..166
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
