ID   ANX11_RABIT             Reviewed;         503 AA.
AC   P33477;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   08-NOV-2023, entry version 128.
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   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Lung;
RX   PubMed=1380798; DOI=10.1016/s0006-291x(05)81537-2;
RA   Tokumitsu H., Mizutani A., Muramatsu M.-A., Yokota T., Arai K., Hidaka H.;
RT   "Molecular cloning of rabbit CAP-50, a calcyclin-associated annexin
RT   protein.";
RL   Biochem. Biophys. Res. Commun. 186:1227-1235(1992).
RN   [2]
RP   PARTIAL PROTEIN SEQUENCE.
RX   PubMed=1533622; DOI=10.1016/s0021-9258(19)50367-2;
RA   Tokumitsu H., Mizutani A., Minami H., Kobayashi R., Hidaka H.;
RT   "A calcyclin-associated protein is a newly identified member of the
RT   Ca2+/phospholipid-binding proteins, annexin family.";
RL   J. Biol. Chem. 267:8919-8924(1992).
RN   [3]
RP   INTERACTION WITH S100A6.
RX   PubMed=9497364; DOI=10.1074/jbc.273.11.6351;
RA   Sudo T., Hidaka H.;
RT   "Regulation of calcyclin (S100A6) binding by alternative splicing in the N-
RT   terminal regulatory domain of annexin XI isoforms.";
RL   J. Biol. Chem. 273:6351-6357(1998).
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 PDCD6 in a calcium-dependent manner (By
CC       similarity). Interacts with KIF23 during cytokinesis (By similarity).
CC       Interacts with S100A6. {ECO:0000250, ECO:0000269|PubMed:9497364}.
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; D10883; BAA01705.1; -; mRNA.
DR   PIR; JH0694; LURB11.
DR   RefSeq; NP_001076208.1; NM_001082739.1.
DR   AlphaFoldDB; P33477; -.
DR   SMR; P33477; -.
DR   STRING; 9986.ENSOCUP00000003940; -.
DR   PaxDb; 9986-ENSOCUP00000003940; -.
DR   GeneID; 100009511; -.
DR   KEGG; ocu:100009511; -.
DR   CTD; 311; -.
DR   eggNOG; KOG0819; Eukaryota.
DR   InParanoid; P33477; -.
DR   OrthoDB; 1500773at2759; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR   GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005819; C:spindle; ISS:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005544; F:calcium-dependent phospholipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0044548; F:S100 protein binding; ISS:UniProtKB.
DR   GO; GO:0032506; P:cytokinetic process; ISS:UniProtKB.
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; Direct protein sequencing; Nucleus;
KW   Reference proteome; Repeat.
FT   CHAIN           1..503
FT                   /note="Annexin A11"
FT                   /id="PRO_0000067512"
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          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          56..178
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        75..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"
SQ   SEQUENCE   503 AA;  54034 MW;  44C15F290770AC9F CRC64;
     MSYPGYPPPP GGYPPAPGGG AWGGAGYPPP SMPPIGLDNV ANYAGQFNQD YLSGMAANMS
     GTFGGANVPP NLYPGAPGGG YPPVPPGGFG QPPPTQPSVP PYGVYPPPGG NPPSGVPSYP
     PFPGAPVPGQ PMPPPGHQPP GPYPGQLPVT YPGQSPVPPP GQQPMPSYPG YPGSGTVTPA
     VPPVQFGNRG TITDASGFDP LRDAEVLRKA MKGFGTDEQA IIDCLGSRSN KQRQQILLSF
     KTAYGKDLIK DLKSELSGNF EKTILALMKT PILFDAYEIK EAIKGAGTDE ACLIEILASR
     SNEHIRELNK AYKTEFKKTL EEAIRSDTSG HFQRLLISLS QGNRDESTNV DMSLVQRDVQ
     ELYAAGENRL GTDESKFNAV LCSRSRAHLV AVFNEYQRMT GRDIEKSICR EMSGDLEQGM
     LAVVKCLKNT PAFFAERLNR AMRGAGTKDR TLIRIMVSRS EIDLLDIRAE YKRMYGKSLY
     HDISGDTSGD YRKILLKICG GND
//