ANX13_MOUSE
ID ANX13_MOUSE Reviewed; 317 AA.
AC Q99JG3;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Annexin A13;
DE AltName: Full=Annexin XIII;
DE AltName: Full=Annexin-13;
GN Name=Anxa13;
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].
RC TISSUE=Small intestine;
RX PubMed=11961095; DOI=10.1093/oxfordjournals.molbev.a004120;
RA Iglesias J.M., Morgan R.O., Jenkins N.A., Copeland N.G., Gilbert D.J.,
RA Fernandez M.-P.;
RT "Comparative genetics and evolution of annexin A13 as the founder gene of
RT vertebrate annexins.";
RL Mol. Biol. Evol. 19:608-618(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
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).
RN [4]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=30610115; DOI=10.1074/jbc.ra118.004571;
RA McCulloch K.M., Yamakawa I., Shifrin D.A. Jr., McConnell R.E.,
RA Foegeding N.J., Singh P.K., Mao S., Tyska M.J., Iverson T.M.;
RT "An alternative N-terminal fold of the intestine-specific annexin A13a
RT induces dimerization and regulates membrane-binding.";
RL J. Biol. Chem. 294:3454-3463(2019).
CC -!- FUNCTION: Binds to membranes enriched in phosphatidylserine or
CC phosphatidylglycerol in a calcium-dependent manner. Half-maximal
CC membrane binding requires about 60 uM calcium. Does not bind to
CC membranes that lack phospholipids with an acidic headgroup.
CC {ECO:0000250|UniProtKB:P27216}.
CC -!- SUBUNIT: Monomer and homodimer. {ECO:0000250|UniProtKB:P27216}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000269|PubMed:30610115}. Cell membrane
CC {ECO:0000250|UniProtKB:P27216}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P27216}. Cytoplasmic vesicle
CC {ECO:0000269|PubMed:30610115}. Note=Myristoylation anchors the protein
CC to the membrane, but the protein also displays calcium-dependent,
CC reversible binding to lipid membranes. {ECO:0000250|UniProtKB:P27216}.
CC -!- TISSUE SPECIFICITY: Detected on the tips of microvilli in small
CC intestine (at protein level). {ECO:0000269|PubMed:30610115}.
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; AJ306451; CAC34623.1; -; mRNA.
DR EMBL; BC013521; AAH13521.1; -; mRNA.
DR RefSeq; NP_081487.1; NM_027211.2.
DR AlphaFoldDB; Q99JG3; -.
DR SMR; Q99JG3; -.
DR IntAct; Q99JG3; 4.
DR PhosphoSitePlus; Q99JG3; -.
DR jPOST; Q99JG3; -.
DR MaxQB; Q99JG3; -.
DR PeptideAtlas; Q99JG3; -.
DR PRIDE; Q99JG3; -.
DR ProteomicsDB; 281891; -.
DR Antibodypedia; 13866; 224 antibodies from 29 providers.
DR DNASU; 69787; -.
DR Ensembl; ENSMUST00000227274; ENSMUSP00000159441; ENSMUSG00000055114.
DR GeneID; 69787; -.
DR KEGG; mmu:69787; -.
DR UCSC; uc007vtm.1; mouse.
DR CTD; 312; -.
DR MGI; MGI:1917037; Anxa13.
DR GeneTree; ENSGT00940000159797; -.
DR InParanoid; Q99JG3; -.
DR OMA; MGNHHAK; -.
DR OrthoDB; 856254at2759; -.
DR BioGRID-ORCS; 69787; 2 hits in 51 CRISPR screens.
DR ChiTaRS; Anxa13; mouse.
DR PRO; PR:Q99JG3; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q99JG3; protein.
DR Bgee; ENSMUSG00000055114; Expressed in duodenum and 49 other tissues.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0019898; C:extrinsic component of membrane; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; ISO:MGI.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; ISO:MGI.
DR GO; GO:1901611; F:phosphatidylglycerol binding; ISO:MGI.
DR GO; GO:0001786; F:phosphatidylserine binding; 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; IPR009166; ANX13.
DR Pfam; PF00191; Annexin; 4.
DR PRINTS; PR00196; ANNEXIN.
DR PRINTS; PR01811; ANNEXINXIII.
DR SMART; SM00335; ANX; 4.
DR SUPFAM; SSF47874; SSF47874; 1.
DR PROSITE; PS00223; ANNEXIN_1; 3.
DR PROSITE; PS51897; ANNEXIN_2; 4.
PE 1: Evidence at protein level;
KW Annexin; Calcium; Calcium/phospholipid-binding; Cell membrane;
KW Cytoplasmic vesicle; Lipoprotein; Membrane; Myristate; Reference proteome;
KW Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P27216"
FT CHAIN 2..317
FT /note="Annexin A13"
FT /id="PRO_0000067515"
FT REPEAT 15..86
FT /note="Annexin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 87..158
FT /note="Annexin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 170..242
FT /note="Annexin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 246..317
FT /note="Annexin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:P27216"
SQ SEQUENCE 317 AA; 35922 MW; 5B43B7564BBAC54A CRC64;
MGNRHAKERS HHHGFDADRD AKKLYKACKG MGTDEAAIIE VLSSRTSEER QQIKQKYKEK
YGKDLEEVLN SELSGNFKKT ALALLDRPNE YAARQLQKAM KGVGTDEAML IEILCTRSNK
EIVAIKEAYQ RLFGRSLESD VKEDTSGNLR KILVSLLQAS RDEEDTVDKE LAGQDAKDLY
DAGEGRWGTD ELAFNEVLAK RSYKQLRATF QAYQILIGKD MEETIEEETS GDLKKAYLTI
VRCAQDLEGY FADLLYKAMK GMGTDEETLI RIIVTRAEVD LQGIKAKFQE KYQKSLSDMV
HSDTSGDFRK LLVALLH
