ID   ANX13_CANLF             Reviewed;         316 AA.
AC   Q29471; Q29472;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 147.
DE   RecName: Full=Annexin A13;
DE   AltName: Full=Annexin XIII {ECO:0000303|PubMed:7896870};
DE   AltName: Full=Annexin-13;
DE   AltName: Full=Intestine-specific annexin;
DE            Short=ISA;
GN   Name=ANXA13; Synonyms=ANX13;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), PROTEIN SEQUENCE OF 150-160;
RP   186-199 AND 310-316, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   STRAIN=Cocker spaniel; TISSUE=Kidney;
RX   PubMed=7896870; DOI=10.1083/jcb.128.6.1043;
RA   Fiedler K., Lafont F., Parton R.G., Simons K.;
RT   "Annexin XIIIb: a novel epithelial specific annexin is implicated in
RT   vesicular traffic to the apical plasma membrane.";
RL   J. Cell Biol. 128:1043-1053(1995).
CC   -!- FUNCTION: [Isoform A]: Binds to membranes enriched in
CC       phosphatidylserine or phosphatidylglycerol in a calcium-dependent
CC       manner. Half-maximal membrane binding requires about 60 uM calcium.
CC       Does not bind to membranes that lack phospholipids with an acidic
CC       headgroup. {ECO:0000250|UniProtKB:P27216}.
CC   -!- FUNCTION: [Isoform B]: Binds to membranes enriched in
CC       phosphatidylserine or phosphatidylglycerol in a calcium-dependent
CC       manner, but requires higher calcium levels for membrane binding than
CC       isoform A. Half-maximal membrane binding requires about 320 uM calcium
CC       (By similarity). May play a role in vesicular traffic to the apical
CC       plasma membrane (Probable). {ECO:0000250|UniProtKB:P27216,
CC       ECO:0000305|PubMed:7896870}.
CC   -!- SUBUNIT: [Isoform A]: Monomer and homodimer.
CC       {ECO:0000250|UniProtKB:P27216}.
CC   -!- SUBCELLULAR LOCATION: Apical cell membrane
CC       {ECO:0000250|UniProtKB:P27216}. Cell membrane
CC       {ECO:0000250|UniProtKB:P27216}; Lipid-anchor
CC       {ECO:0000250|UniProtKB:P27216}. Cytoplasmic vesicle
CC       {ECO:0000250|UniProtKB:Q99JG3}. 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   -!- SUBCELLULAR LOCATION: [Isoform B]: Cytoplasmic vesicle
CC       {ECO:0000269|PubMed:7896870}. Note=Enriched in apical vesicles.
CC       {ECO:0000269|PubMed:7896870}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=A; Synonyms=Anx13A;
CC         IsoId=Q29471-1; Sequence=Displayed;
CC       Name=B; Synonyms=Anx13B;
CC         IsoId=Q29471-2; Sequence=VSP_000290;
CC   -!- TISSUE SPECIFICITY: [Isoform B]: Detected in intestine, and at much
CC       lower levels also in kidney (at protein level).
CC       {ECO:0000269|PubMed:7896870}.
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; X80208; CAA56506.1; -; mRNA.
DR   EMBL; X80209; CAA56507.1; -; mRNA.
DR   PIR; A57076; A57076.
DR   PIR; B57076; B57076.
DR   RefSeq; NP_001003255.1; NM_001003255.1. [Q29471-2]
DR   RefSeq; XP_005627863.1; XM_005627806.1. [Q29471-1]
DR   AlphaFoldDB; Q29471; -.
DR   SMR; Q29471; -.
DR   BioGRID; 139851; 1.
DR   STRING; 9612.ENSCAFP00000001437; -.
DR   PaxDb; Q29471; -.
DR   PRIDE; Q29471; -.
DR   Ensembl; ENSCAFT00030013715; ENSCAFP00030011970; ENSCAFG00030007468. [Q29471-1]
DR   Ensembl; ENSCAFT00030013884; ENSCAFP00030012120; ENSCAFG00030007468. [Q29471-2]
DR   Ensembl; ENSCAFT00845017793; ENSCAFP00845013860; ENSCAFG00845010107. [Q29471-1]
DR   GeneID; 403935; -.
DR   KEGG; cfa:403935; -.
DR   CTD; 312; -.
DR   VEuPathDB; HostDB:ENSCAFG00845010107; -.
DR   eggNOG; KOG0819; Eukaryota.
DR   GeneTree; ENSGT00940000159797; -.
DR   HOGENOM; CLU_025300_0_2_1; -.
DR   InParanoid; Q29471; -.
DR   OMA; MGNHHAK; -.
DR   OrthoDB; 856254at2759; -.
DR   TreeFam; TF105452; -.
DR   Proteomes; UP000002254; Chromosome 13.
DR   Bgee; ENSCAFG00000001015; Expressed in jejunum and 39 other tissues.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR   GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR   GO; GO:0070382; C:exocytic vesicle; IDA:CAFA.
DR   GO; GO:0045121; C:membrane raft; IDA: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:0042997; P:negative regulation of Golgi to plasma membrane protein transport; IDA:UniProtKB.
DR   GO; GO:0042998; P:positive regulation of Golgi to plasma membrane protein transport; IDA: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; 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   Alternative splicing; Annexin; Calcium; Calcium/phospholipid-binding;
KW   Cell membrane; Cytoplasmic vesicle; Direct protein sequencing; Lipoprotein;
KW   Membrane; Myristate; Reference proteome; Repeat.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P27216"
FT   CHAIN           2..316
FT                   /note="Annexin A13"
FT                   /id="PRO_0000067513"
FT   REPEAT          14..85
FT                   /note="Annexin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT   REPEAT          86..157
FT                   /note="Annexin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT   REPEAT          169..241
FT                   /note="Annexin 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT   REPEAT          245..316
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"
FT   VAR_SEQ         5
FT                   /note="H -> HSQSYSLSEGSQQLPKGDIQPSAAVQPLSHPSGSGEPEAQQP (in
FT                   isoform B)"
FT                   /evidence="ECO:0000303|PubMed:7896870"
FT                   /id="VSP_000290"
SQ   SEQUENCE   316 AA;  35479 MW;  FD0B34AE0B6C8441 CRC64;
     MGNRHAKAKS HHGFDVDHDA KKLNKACKGM GTDEAAIIEI LSSRTSDERQ QIKQKYKATY
     GKDLEEVFKS DLSGNFEKTA LALLDRPSEY DARQLQKAMK GLGTDEAVLI EILCTRTNKE
     IMAIKEAYQR LFDRSLESDV KADTSGNLKA ILVSLLQANR DEGDDVDKDL AGQDAKDLYD
     AGDGRWGTDE LAFNEVLAKR SHKQLRATFQ AYQILIDKDI EEAIEAETSG DLQKAYLTLV
     RCARDQEGYF ADRLYKSMKG TGTDEETLIH IIVTRAEVDL QGIKAKFQEK YQKSLSDMVR
     SDTSGDFQKL LVALLH