ANX12_COLLI
ID ANX12_COLLI Reviewed; 343 AA.
AC Q92040; Q92041;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Annexin A1 isoform p37;
DE AltName: Full=Annexin I isoform p37;
DE AltName: Full=Calpactin II;
DE AltName: Full=Calpactin-2;
DE AltName: Full=Chromobindin-9;
DE AltName: Full=Lipocortin I;
DE AltName: Full=Phospholipase A2 inhibitory protein;
GN Name=CP37;
OS Columba livia (Rock dove).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Columba.
OX NCBI_TaxID=8932;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 13-50, AND PHOSPHORYLATION
RP AT TYR-21 AND SER-24.
RC STRAIN=White Carneau; TISSUE=Cropsac;
RX PubMed=1388165; DOI=10.1016/s0021-9258(18)41751-6;
RA Haigler H.T., Mangili J.A., Gao Y., Jones J., Horseman N.D.;
RT "Identification and characterization of columbid annexin Icp37. Insights
RT into the evolution of annexin I phosphorylation sites.";
RL J. Biol. Chem. 267:19123-19129(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-154.
RC STRAIN=N41; TISSUE=Liver;
RX PubMed=8206371; DOI=10.1016/0378-1119(94)90094-9;
RA Gao Y., Horseman N.D.;
RT "Structural and functional divergences of the columbid annexin I-encoding
RT cp37 and cp35 genes.";
RL Gene 143:179-186(1994).
CC -!- FUNCTION: Calcium/phospholipid-binding protein which promotes membrane
CC fusion and is involved in exocytosis. This protein regulates
CC phospholipase A2 activity. It seems to bind from two to four calcium
CC ions with high affinity.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Cell projection, cilium {ECO:0000250}. Basolateral cell membrane
CC {ECO:0000250}. Note=Found in the cilium, nucleus and basolateral cell
CC membrane of ciliated cells in the tracheal endothelium. Found in the
CC cytoplasm of type II pneumocytes and alveolar macrophages.
CC {ECO:0000250}.
CC -!- DOMAIN: A pair of annexin repeats may form one binding site for calcium
CC and phospholipid.
CC -!- PTM: Phosphorylated by protein kinase C and epidermal growth factor
CC receptor/kinase. {ECO:0000269|PubMed:1388165}.
CC -!- PTM: The N-terminus is blocked.
CC -!- MISCELLANEOUS: In pigeons, two isoforms of annexin-I are encoded by the
CC differentially regulated genes CP35 and CP37.
CC -!- SIMILARITY: Belongs to the annexin family. {ECO:0000255|PROSITE-
CC ProRule:PRU01245, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA49447.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M91008; AAA49447.1; ALT_INIT; mRNA.
DR EMBL; L02504; AAA20674.1; -; Genomic_DNA.
DR PIR; A44118; A44118.
DR RefSeq; NP_001269749.1; NM_001282820.1.
DR AlphaFoldDB; Q92040; -.
DR SMR; Q92040; -.
DR STRING; 8932.XP_005504281.1; -.
DR iPTMnet; Q92040; -.
DR PRIDE; Q92040; -.
DR GeneID; 102093126; -.
DR KEGG; clv:102093126; -.
DR eggNOG; KOG0819; Eukaryota.
DR OrthoDB; 856254at2759; -.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0019834; F:phospholipase A2 inhibitor activity; IEA:UniProtKB-KW.
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; IPR002388; ANX1.
DR PANTHER; PTHR10502:SF17; PTHR10502:SF17; 1.
DR Pfam; PF00191; Annexin; 4.
DR PRINTS; PR00196; ANNEXIN.
DR PRINTS; PR00197; ANNEXINI.
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 Annexin; Calcium; Calcium/phospholipid-binding; Cell membrane;
KW Cell projection; Cilium; Cytoplasm; Direct protein sequencing;
KW Isopeptide bond; Membrane; Nucleus; Phospholipase A2 inhibitor;
KW Phosphoprotein; Repeat.
FT CHAIN 1..343
FT /note="Annexin A1 isoform p37"
FT /id="PRO_0000067468"
FT REPEAT 38..109
FT /note="Annexin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 110..181
FT /note="Annexin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 193..265
FT /note="Annexin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 269..340
FT /note="Annexin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT MOD_RES 21
FT /note="Phosphotyrosine; by EGFR; in vitro"
FT /evidence="ECO:0000269|PubMed:1388165"
FT MOD_RES 24
FT /note="Phosphoserine; by PKC; in vitro"
FT /evidence="ECO:0000269|PubMed:1388165"
FT CROSSLNK 19
FT /note="Isoglutamyl lysine isopeptide (Gln-Lys) (interchain
FT with K-?)"
FT /evidence="ECO:0000250"
FT CONFLICT 74..75
FT /note="HR -> QQ (in Ref. 2; AAA20674)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 343 AA; 38849 MW; 49A621A92BCEDFDC CRC64;
MAMVSEFLKQ AWFMEHQEQE YIKSVKGGPV VPQQQPNFDP SADVVALEKA MTAKGVDEAT
IIDIMTKRTN AQRHRIKAAY QKAKGKSLEE AMKRVLKSHL EDVVVALLKT PAQFDAEELR
ACMKGLGTDE DTLIEILASR SNKEIREASR YYKEVLKRDL TQDIISDTSG HFQKALVVLA
KGDRCEDPHV NDDLADNDAR ALYEAGEQKK GTDVNVFVTV LTARSYPHLR RVFQKYTKYS
KHDMNKVVDM ELKGDIEKCL TALVKCATSK PAFFAEKLHL AMKGFGTRHK DLIRIMVSRH
EVDMNEIKCY YKKMYGISLC QAIMDDLKGD YETILVALCG SDN
