ID   ANX11_COLLI             Reviewed;         341 AA.
AC   P14950;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   25-MAY-2022, entry version 103.
DE   RecName: Full=Annexin A1 isoform p35;
DE   AltName: Full=Annexin I isoform p35;
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=CP35;
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].
RX   PubMed=2526923; DOI=10.1210/mend-3-5-773;
RA   Horseman N.D.;
RT   "A prolactin-inducible gene product which is a member of the
RT   calpactin/lipocortin family.";
RL   Mol. Endocrinol. 3:773-779(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-53.
RX   PubMed=1832409; DOI=10.1016/0378-1119(91)90272-d;
RA   Hitti Y.S., Horseman N.D.;
RT   "Structure of the gene encoding columbid annexin Icp35.";
RL   Gene 103:185-192(1991).
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   -!- INDUCTION: Major prolactin-inducible protein in pigeon cropsac.
CC   -!- DOMAIN: A pair of annexin repeats may form one binding site for calcium
CC       and phospholipid.
CC   -!- PTM: In contrast to mammalian homologs, does not contain a tyrosine
CC       phosphorylation site in the N-terminal part.
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}.
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DR   EMBL; M22635; AAA49448.1; -; mRNA.
DR   PIR; A40153; LUPY1.
DR   RefSeq; NP_001269775.1; NM_001282846.1.
DR   AlphaFoldDB; P14950; -.
DR   SMR; P14950; -.
DR   STRING; 8932.XP_005504282.1; -.
DR   PRIDE; P14950; -.
DR   GeneID; 102093306; -.
DR   KEGG; clv:102093306; -.
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; 3.
DR   PROSITE; PS51897; ANNEXIN_2; 4.
PE   2: Evidence at transcript level;
KW   Annexin; Calcium; Calcium/phospholipid-binding; Cell membrane;
KW   Cell projection; Cilium; Cytoplasm; Membrane; Nucleus;
KW   Phospholipase A2 inhibitor; Repeat.
FT   CHAIN           1..341
FT                   /note="Annexin A1 isoform p35"
FT                   /id="PRO_0000067467"
FT   REPEAT          37..108
FT                   /note="Annexin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT   REPEAT          109..180
FT                   /note="Annexin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT   REPEAT          192..263
FT                   /note="Annexin 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT   REPEAT          267..338
FT                   /note="Annexin 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
SQ   SEQUENCE   341 AA;  38451 MW;  AB6B5CF7F3618DA2 CRC64;
     MAVVSEFLKQ AWFMENLEQE CIKCTQCVHG VPQQTNFDPS ADVVALEKAM TAKGVDEATI
     IDIMTTRTNA QRPRIKAAYH KAKGKSLEEA MKRVLKSHLE DVVVALLKTP AQFDAEELRA
     CMKGHGTDED TLIEILASRN NKEIREACRY YKEVLKRDLT QDIISDTSGD FQKALVSLAK
     ADRCENPHVN DELAEKDARA LYEAGEQKKG TDINVFVTVL TARSYPHSEV FQKYTKYSKH
     DMNKAVDMEM KGDIEKCLTA LVKCATSKPA FFAEKLHMAM KGFGTQHRDL IRIMVSRHEV
     DMNEIKGYYK KMYGISLCQA IMDELKGGYE TILVALCGSD N