ANX11_RABIT
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 25-MAY-2022, entry version 125.
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 GeneID; 100009511; -.
DR KEGG; ocu:100009511; -.
DR CTD; 311; -.
DR eggNOG; KOG0819; Eukaryota.
DR InParanoid; P33477; -.
DR OrthoDB; 856254at2759; -.
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; -; 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; 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