ID   UCAL_HORSE              Reviewed;         180 AA.
AC   Q28388;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=Uterocalin;
DE   AltName: Full=Concepticalin;
DE   AltName: Full=Equicalin;
DE   AltName: Full=Lipocalin P19;
DE   Flags: Precursor;
OS   Equus caballus (Horse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX   NCBI_TaxID=9796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 19-42, TISSUE SPECIFICITY,
RP   AND SUBCELLULAR LOCATION.
RC   TISSUE=Endometrium;
RX   PubMed=8947478; DOI=10.1042/bj3200137;
RA   Crossett B., Allen W.R., Stewart F.;
RT   "A 19 kDa protein secreted bythe endometrium of the mare is a novel member
RT   of the lipocalin family.";
RL   Biochem. J. 320:137-143(1996).
RN   [2]
RP   TISSUE SPECIFICITY, AND FUNCTION.
RX   PubMed=9716544; DOI=10.1095/biolreprod59.3.483;
RA   Crossett B., Suire S., Herrler A., Allen W.R., Stewart F.;
RT   "Transfer of a uterine lipocalin from the endometrium of the mare to the
RT   developing equine conceptus.";
RL   Biol. Reprod. 59:483-490(1998).
RN   [3]
RP   FUNCTION, AND MUTAGENESIS OF TRP-150.
RX   PubMed=11368763; DOI=10.1042/0264-6021:3560369;
RA   Suire S., Stewart F., Beauchamp J., Kennedy M.W.;
RT   "Uterocalin, a lipocalin provisioning the preattachment equine conceptus:
RT   fatty acid and retinol binding properties, and structural
RT   characterization.";
RL   Biochem. J. 356:369-376(2001).
CC   -!- FUNCTION: Binds fatty acids and retinol. Is specialized for the
CC       preattachment embryo. May be important to maintain the pregnancy and
CC       may transport small hydrophobic ligands from mother to the developing
CC       embryo. {ECO:0000269|PubMed:11368763, ECO:0000269|PubMed:9716544}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8947478}.
CC   -!- TISSUE SPECIFICITY: Expressed in glandular and lumenal epithelia of the
CC       endometrium. Is transferred to the embryonic capsule, the conceptus and
CC       the yolk sac. {ECO:0000269|PubMed:8947478, ECO:0000269|PubMed:9716544}.
CC   -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC       {ECO:0000305}.
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DR   EMBL; X98459; CAA67099.1; -; mRNA.
DR   RefSeq; NP_001075978.2; NM_001082509.2.
DR   AlphaFoldDB; Q28388; -.
DR   SMR; Q28388; -.
DR   STRING; 9796.ENSECAP00000050030; -.
DR   PaxDb; Q28388; -.
DR   GeneID; 100034213; -.
DR   KEGG; ecb:100034213; -.
DR   CTD; 100034213; -.
DR   OrthoDB; 1271544at2759; -.
DR   Proteomes; UP000002281; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005549; F:odorant binding; IBA:GO_Central.
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; IPR000566; Lipocln_cytosolic_FA-bd_dom.
DR   InterPro; IPR002971; Maj_urinary.
DR   PANTHER; PTHR11430; PTHR11430; 1.
DR   Pfam; PF00061; Lipocalin; 1.
DR   PRINTS; PR01221; MAJORURINARY.
DR   SUPFAM; SSF50814; SSF50814; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Reference proteome; Secreted; Signal; Transport.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000269|PubMed:8947478"
FT   CHAIN           19..180
FT                   /note="Uterocalin"
FT                   /id="PRO_0000249685"
FT   CARBOHYD        101
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        82..175
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         150
FT                   /note="W->E: No effect."
FT                   /evidence="ECO:0000269|PubMed:11368763"
SQ   SEQUENCE   180 AA;  20805 MW;  892BB394BEF93417 CRC64;
     MNLLLLAMGL ILPRRPHALH MGPGDPNFDE KLVKGKWFSV ALASNEPKFI AKDTDMKFFI
     HKIQVTPESL QFHFHRKVRG MCVPTMMTAH KTKKKFQYTV NHSGHKTIFL EKVDPKHFVI
     FCAHSMKHGK ETVVVTLFSR TPTVSPDVMW MFKKYCKTHG IHTSNIVDLT QTDRCLHARH