ID   LIPO_RHIMB              Reviewed;         183 AA.
AC   Q01584;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Lipocalin;
DE   Flags: Precursor;
OS   Rhinella marina (Cane toad) (Bufo marinus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Hyloidea; Bufonidae; Rhinella.
OX   NCBI_TaxID=8386;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 21-36; 38-40; 87-93;
RP   106-113 AND 156-161.
RC   TISSUE=Choroid plexus;
RX   PubMed=1385415; DOI=10.1016/s0021-9258(18)50072-7;
RA   Achen M.G., Harms P.J., Thomas T., Richardson S.J., Wettenhall R.E.H.,
RA   Schreiber G.;
RT   "Protein synthesis at the blood-brain barrier. The major protein secreted
RT   by amphibian choroid plexus is a lipocalin.";
RL   J. Biol. Chem. 267:23170-23174(1992).
CC   -!- FUNCTION: Might have a transport function across the blood brain
CC       barrier. Is supposed to have similar functions as transthyretin which
CC       must have evolved after the stage of the amphibians in evolution.
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Secreted. Note=Found in cerebrospinal fluid.
CC   -!- TISSUE SPECIFICITY: Expressed mainly in choroid plexus. Much lower
CC       expression in other brain areas, and absent from liver.
CC   -!- DEVELOPMENTAL STAGE: Expressed throughout amphibian metamorphosis.
CC   -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC       {ECO:0000305}.
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DR   EMBL; X67952; CAA48138.1; -; mRNA.
DR   EMBL; L06806; AAA48554.1; -; mRNA.
DR   PIR; A44456; S25465.
DR   AlphaFoldDB; Q01584; -.
DR   SMR; Q01584; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0036094; F:small molecule binding; IEA:InterPro.
DR   Gene3D; 2.40.128.20; -; 1.
DR   InterPro; IPR012674; Calycin.
DR   InterPro; IPR002345; Lipocalin.
DR   InterPro; IPR022272; Lipocalin_CS.
DR   InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
DR   InterPro; IPR002972; PstgldnD_synth.
DR   PANTHER; PTHR11430; PTHR11430; 1.
DR   PANTHER; PTHR11430:SF86; PTHR11430:SF86; 1.
DR   Pfam; PF00061; Lipocalin; 1.
DR   SUPFAM; SSF50814; SSF50814; 1.
DR   PROSITE; PS00213; LIPOCALIN; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000269|PubMed:1385415"
FT   CHAIN           21..183
FT                   /note="Lipocalin"
FT                   /id="PRO_0000017988"
FT   DISULFID        83..179
SQ   SEQUENCE   183 AA;  20608 MW;  79017CDB1BCF2911 CRC64;
     MKGLVLSFAL VALSALCVYG DVPIQPDFQE DKILGKWYGI GLASNSNWFQ SKKQQLKMCT
     TVITPTADGN LDVVATFPKL DRCEKKSMTY IKTEQPGRFL SKSPRYGSDH VIRVVESNYD
     EYTLMHTIKT KGNEVNTIVS LFGRRKTLSP ELLDKFQQFA KEQGLTDDNI LILPQTDSCM
     SEV