ANX11_BOVIN
ID ANX11_BOVIN Reviewed; 503 AA.
AC P27214; P27215; Q0VD55;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 146.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Chondrocyte;
RX PubMed=1372001; DOI=10.1016/s0021-9258(18)42782-2;
RA Towle C.A., Treadwell B.V.;
RT "Identification of a novel mammalian annexin. cDNA cloning, sequence
RT analysis, and ubiquitous expression of the annexin XI gene.";
RL J. Biol. Chem. 267:5416-5423(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
RC TISSUE=Cartilage;
RX PubMed=1535225; DOI=10.1016/0167-4781(92)90084-d;
RA Towle C.A., Weissbach L., Treadwell B.V.;
RT "Alternatively spliced annexin XI transcripts encode proteins that differ
RT near the amino-terminus.";
RL Biochim. Biophys. Acta 1131:223-226(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Hereford; TISSUE=Heart ventricle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PROTEIN SEQUENCE OF 213-226; 319-337; 441-459 AND 478-497.
RX PubMed=1618851; DOI=10.1016/s0021-9258(18)42239-9;
RA Mizutani A., Usuda N., Tokumitsu H., Minami H., Yasui K., Kobayashi R.,
RA Hidaka H.;
RT "CAP-50, a newly identified annexin, localizes in nuclei of cultured
RT fibroblast 3Y1 cells.";
RL J. Biol. Chem. 267:13498-13504(1992).
RN [5]
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: Binds specifically to calcyclin in a calcium-dependent
CC manner. Required for midbody formation and completion of the terminal
CC phase of cytokinesis. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with PDCD6 in a calcium-dependent manner (By
CC similarity). Interacts with KIF23 during cytokinesis (By similarity).
CC Isoform 1 but not isoform 2 interacts with S100A6. {ECO:0000250,
CC 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P27214-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P27214-2; Sequence=VSP_000289;
CC -!- TISSUE SPECIFICITY: Expressed in a wide variety of tissues.
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}.
CC -!- CAUTION: The subcellular location study was carried out using a rat
CC fibroblast cell line. {ECO:0000305}.
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DR EMBL; M82802; AAA30379.1; -; mRNA.
DR EMBL; Z11742; CAA77801.1; -; mRNA.
DR EMBL; BC119826; AAI19827.1; -; mRNA.
DR PIR; A42113; LUBO11.
DR PIR; S23447; S23447.
DR RefSeq; NP_776927.1; NM_174502.2. [P27214-2]
DR AlphaFoldDB; P27214; -.
DR SMR; P27214; -.
DR PaxDb; P27214; -.
DR PeptideAtlas; P27214; -.
DR PRIDE; P27214; -.
DR GeneID; 282142; -.
DR KEGG; bta:282142; -.
DR CTD; 311; -.
DR eggNOG; KOG0819; Eukaryota.
DR InParanoid; P27214; -.
DR OrthoDB; 856254at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProt.
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; IBA:GO_Central.
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 GO; GO:0006909; P:phagocytosis; IBA:GO_Central.
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; Alternative splicing; Annexin; Calcium;
KW Calcium/phospholipid-binding; Cell cycle; Cell division; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; Nucleus; Reference proteome;
KW Repeat.
FT CHAIN 1..503
FT /note="Annexin A11"
FT /id="PRO_0000067509"
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..197
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 COMPBIAS 167..192
FT /note="Polar 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 VAR_SEQ 20..56
FT /note="GGAWGGAGYPPPTMPPIGLDNVANYAGQFNQDYLSGV -> VPELESHAGGP
FT QGLFAAMDRAVSDGPAMMLAAVLLVRAT (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_000289"
FT CONFLICT 113
FT /note="T -> P (in Ref. 3; AAI19827)"
FT /evidence="ECO:0000305"
FT CONFLICT 326
FT /note="S -> G (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 334
FT /note="R -> Q (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 455
FT /note="I -> D (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 503 AA; 54018 MW; 3AF6503CCA6D05A1 CRC64;
MSYPGYPPPA GGYPPGAPGG GAWGGAGYPP PTMPPIGLDN VANYAGQFNQ DYLSGVAANM
SGTFGGANVP NLYPGAPGGG YPPVPPGGFG QPPPAQQPVP SYGMYPPPGG NPTSGMPSYP
PYPGAPVPGQ PMLPPGQQPP GVYPGQPPMT YPGQSPVPPP GQQPVPSYPG YSGSGTVTPA
VSPAQFGNRG TITDASGFDP LRDAEVLRKA MKGFGTDEQA IIDCLGSRSN KQRQQILLSF
KTAYGKDLIK DLKSELSGNF EKTILALMKT PVLFDAYEIK EAIKGAGTDE ACLIEILASR
SNEHIRELNR VYKTEFKKTL EEAIRSDTSG HFQRLLISLS QGNRDESTNV DMTLVQRDVQ
ELYAAGENRL GTDESKFNAI LCSRSRAHLV AVFNEYQRMT GRDIEKSICR EMSGDLEQGM
LAVVKCLKNT PAFFAERLNK AMRGAGTKDR TLIRIMVSRS EIDLLDIRAE YKRLYGKSLY
HDITGDTSGD YRKILLKICG GND
