UTER_RAT
ID UTER_RAT Reviewed; 96 AA.
AC P17559;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Uteroglobin;
DE AltName: Full=Clara cell phospholipid-binding protein;
DE Short=CCPBP;
DE AltName: Full=Clara cells 10 kDa secretory protein;
DE Short=CC10;
DE AltName: Full=PCB-binding protein;
DE AltName: Full=Secretoglobin family 1A member 1;
DE Flags: Precursor;
GN Name=Scgb1a1; Synonyms=Cc10, Ugb, Utg;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Katyal S.L., Singh G., Brown W.E., Kennedy A.L., Squeglia N.,
RA Wong-Chong M.-L.;
RT "Clara cell secretory (10 kDaltons) protein: amino acid and cDNA nucleotide
RT sequences and developmental expression.";
RL Prog. Respir. Res. 25:29-35(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2115524; DOI=10.1016/s0021-9258(19)38399-1;
RA Nordlund-Moeller L., Andersson O., Ahlgren R., Schilling J., Gillner M.,
RA Gustafsson J.-A., Lund J.;
RT "Cloning, structure, and expression of a rat binding protein for
RT polychlorinated biphenyls. Homology to the hormonally regulated
RT progesterone-binding protein uteroglobin.";
RL J. Biol. Chem. 265:12690-12693(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-18.
RX PubMed=2349092; DOI=10.1093/nar/18.10.2939;
RA Hagen G., Wolf M., Katyal S.L., Singh G., Beato M., Suske G.;
RT "Tissue-specific expression, hormonal regulation and 5'-flanking gene
RT region of the rat Clara cell 10 kDa protein: comparison to rabbit
RT uteroglobin.";
RL Nucleic Acids Res. 18:2939-2946(1990).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 20-96, AND SUBUNIT.
RX PubMed=1560460; DOI=10.1016/0022-2836(92)91006-b;
RA Umland T.C., Swaminathan S., Furey W., Singh G., Pletcher J., Sax M.;
RT "Refined structure of rat Clara cell 17 kDa protein at 3.0-A resolution.";
RL J. Mol. Biol. 224:441-448(1992).
RN [6]
RP STRUCTURE BY NMR.
RX PubMed=7583672; DOI=10.1038/nsb1195-983;
RA Haerd T., Barnes H.J., Larsson C., Gustafsson J.-A., Lund J.;
RT "Solution structure of a mammalian PCB-binding protein in complex with a
RT PCB.";
RL Nat. Struct. Biol. 2:983-989(1995).
CC -!- FUNCTION: Binds phosphatidylcholine, phosphatidylinositol,
CC polychlorinated biphenyls (PCB) and weakly progesterone, potent
CC inhibitor of phospholipase A2.
CC -!- SUBUNIT: Antiparallel homodimer; disulfide-linked (PubMed:1560460).
CC Interaction with LMBR1L is controversial (By similarity).
CC {ECO:0000250|UniProtKB:P11684, ECO:0000269|PubMed:1560460}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Clara cells (nonciliated cells of the surface
CC epithelium of the pulmonary airways).
CC -!- INDUCTION: By glucocorticoids.
CC -!- SIMILARITY: Belongs to the secretoglobin family. {ECO:0000305}.
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DR EMBL; J05536; AAA41817.1; -; mRNA.
DR EMBL; BC069174; AAH69174.1; -; mRNA.
DR EMBL; X51318; CAA35701.1; -; Genomic_DNA.
DR PIR; A36581; A36581.
DR RefSeq; NP_037183.1; NM_013051.1.
DR PDB; 1CCD; X-ray; 3.00 A; A=20-96.
DR PDB; 1UTR; NMR; -; A/B=1-96.
DR PDBsum; 1CCD; -.
DR PDBsum; 1UTR; -.
DR AlphaFoldDB; P17559; -.
DR SMR; P17559; -.
DR STRING; 10116.ENSRNOP00000027342; -.
DR iPTMnet; P17559; -.
DR PhosphoSitePlus; P17559; -.
DR PaxDb; P17559; -.
DR Ensembl; ENSRNOT00000027342; ENSRNOP00000027342; ENSRNOG00000020196.
DR GeneID; 25575; -.
DR KEGG; rno:25575; -.
DR UCSC; RGD:3934; rat.
DR CTD; 7356; -.
DR RGD; 3934; Scgb1a1.
DR eggNOG; ENOG502SXFT; Eukaryota.
DR GeneTree; ENSGT00940000155073; -.
DR HOGENOM; CLU_166234_1_0_1; -.
DR InParanoid; P17559; -.
DR OMA; MKIAITI; -.
DR OrthoDB; 1608982at2759; -.
DR PhylomeDB; P17559; -.
DR TreeFam; TF338407; -.
DR EvolutionaryTrace; P17559; -.
DR PRO; PR:P17559; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000020196; Expressed in lung and 13 other tissues.
DR Genevisible; P17559; RN.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0005635; C:nuclear envelope; IDA:RGD.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IDA:RGD.
DR GO; GO:0030141; C:secretory granule; IDA:RGD.
DR GO; GO:0019834; F:phospholipase A2 inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0097160; F:polychlorinated biphenyl binding; IPI:RGD.
DR GO; GO:0032689; P:negative regulation of interferon-gamma production; ISO:RGD.
DR GO; GO:0032696; P:negative regulation of interleukin-13 production; ISO:RGD.
DR GO; GO:0032713; P:negative regulation of interleukin-4 production; ISO:RGD.
DR GO; GO:0032714; P:negative regulation of interleukin-5 production; ISO:RGD.
DR GO; GO:0042130; P:negative regulation of T cell proliferation; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0050727; P:regulation of inflammatory response; ISO:RGD.
DR GO; GO:0043488; P:regulation of mRNA stability; ISO:RGD.
DR GO; GO:0034097; P:response to cytokine; IMP:RGD.
DR GO; GO:0071774; P:response to fibroblast growth factor; IEP:RGD.
DR GO; GO:0051384; P:response to glucocorticoid; IEP:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0010033; P:response to organic substance; IEP:RGD.
DR GO; GO:0010193; P:response to ozone; IEP:RGD.
DR GO; GO:0034021; P:response to silicon dioxide; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR GO; GO:0042098; P:T cell proliferation; IEA:Ensembl.
DR CDD; cd00633; Secretoglobin; 1.
DR InterPro; IPR016126; Secretoglobin.
DR InterPro; IPR043215; Secretoglobin_1C-like.
DR InterPro; IPR035960; Secretoglobin_sf.
DR InterPro; IPR000329; Uteroglobin.
DR PANTHER; PTHR10136; PTHR10136; 1.
DR Pfam; PF01099; Uteroglobin; 1.
DR PRINTS; PR00486; UTEROGLOBIN.
DR SUPFAM; SSF48201; SSF48201; 1.
DR PROSITE; PS51311; SCGB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Phospholipase A2 inhibitor;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT CHAIN 20..96
FT /note="Uteroglobin"
FT /id="PRO_0000036367"
FT DISULFID 24
FT /note="Interchain (with C-90)"
FT DISULFID 90
FT /note="Interchain (with C-24)"
FT HELIX 25..34
FT /evidence="ECO:0007829|PDB:1CCD"
FT HELIX 39..46
FT /evidence="ECO:0007829|PDB:1CCD"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:1CCD"
FT HELIX 53..68
FT /evidence="ECO:0007829|PDB:1CCD"
FT HELIX 71..84
FT /evidence="ECO:0007829|PDB:1CCD"
FT TURN 88..90
FT /evidence="ECO:0007829|PDB:1CCD"
SQ SEQUENCE 96 AA; 10449 MW; 1A12988677B9EBEF CRC64;
MKIAITITVL MLSICCSSAS SDICPGFLQV LEALLLGSES NYEAALKPFN PASDLQNAGT
QLKRLVDTLP QETRINIVKL TEKILTSPLC EQDLRV
