LCN12_RAT
ID LCN12_RAT Reviewed; 193 AA.
AC B3EY83; D3ZI71;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 2.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Epididymal-specific lipocalin-12;
DE Flags: Precursor;
GN Name=Lcn12;
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].
RC STRAIN=Sprague-Dawley;
RA Liu Q., Chen W., Guo C., Lin D., Zhang Y.-L.;
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [3]
RP STRUCTURE BY NMR OF 19-193 OF MUTANT ALA-166, MUTAGENESIS OF CYS-166,
RP FUNCTION, SUBUNIT, IDENTIFICATION BY MASS SPECTROMETRY, AND DISULFIDE BOND.
RX PubMed=20692383; DOI=10.1016/j.bbapap.2010.07.020;
RA Peng Y., Liu J., Liu Q., Yao Y., Guo C., Zhang Y., Lin D.;
RT "Conformational and biochemical characterization of a rat epididymis-
RT specific lipocalin 12 expressed in Escherichia coli.";
RL Biochim. Biophys. Acta 1804:2102-2110(2010).
RN [4]
RP STRUCTURE BY NMR OF 19-193 OF MUTANT ALA-166, MUTAGENESIS OF CYS-166, AND
RP DISULFIDE BOND.
RX PubMed=21538546; DOI=10.1002/prot.23031;
RA Peng Y., Zhang X., Liu J., Liu Q., Guo C., Zhang Y., Lin D.;
RT "Solution structure of the protein lipocalin 12 from rat epididymis.";
RL Proteins 79:2316-2320(2011).
CC -!- FUNCTION: Binds all-trans retinoic acid and may act as a retinoid
CC carrier protein within the epididymis. May play a role in male
CC fertility. {ECO:0000269|PubMed:20692383}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:20692383}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABG24235.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; DQ537492; ABG24235.1; ALT_INIT; mRNA.
DR PDB; 2L5P; NMR; -; A=19-193.
DR PDBsum; 2L5P; -.
DR AlphaFoldDB; B3EY83; -.
DR BMRB; B3EY83; -.
DR SMR; B3EY83; -.
DR STRING; 10116.ENSRNOP00000020997; -.
DR GlyGen; B3EY83; 2 sites.
DR PaxDb; B3EY83; -.
DR Ensembl; ENSRNOT00000020997; ENSRNOP00000020997; ENSRNOG00000028701.
DR UCSC; RGD:1589474; rat.
DR RGD; 1589474; Lcn12.
DR eggNOG; ENOG502S9R9; Eukaryota.
DR GeneTree; ENSGT00440000034309; -.
DR InParanoid; B3EY83; -.
DR Reactome; R-RNO-804914; Transport of fatty acids.
DR PRO; PR:B3EY83; -.
DR Proteomes; UP000002494; Chromosome 3.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0001972; F:retinoic acid binding; IDA:UniProtKB.
DR Gene3D; 2.40.128.20; -; 1.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR003087; LCN2/LCN12.
DR InterPro; IPR002345; Lipocalin.
DR InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
DR PANTHER; PTHR11430; PTHR11430; 1.
DR Pfam; PF00061; Lipocalin; 1.
DR PRINTS; PR01275; NGELATINASE.
DR SUPFAM; SSF50814; SSF50814; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Glycoprotein; Reference proteome; Secreted;
KW Signal; Transport.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..193
FT /note="Epididymal-specific lipocalin-12"
FT /id="PRO_0000415891"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 172
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 88..193
FT /evidence="ECO:0000269|PubMed:20692383,
FT ECO:0000269|PubMed:21538546"
FT MUTAGEN 166
FT /note="C->A: Abolishes intermolecular disulfide bond
FT formation."
FT /evidence="ECO:0000269|PubMed:20692383,
FT ECO:0000269|PubMed:21538546"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:2L5P"
FT HELIX 36..39
FT /evidence="ECO:0007829|PDB:2L5P"
FT STRAND 41..50
FT /evidence="ECO:0007829|PDB:2L5P"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:2L5P"
FT STRAND 65..70
FT /evidence="ECO:0007829|PDB:2L5P"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:2L5P"
FT STRAND 76..84
FT /evidence="ECO:0007829|PDB:2L5P"
FT STRAND 87..97
FT /evidence="ECO:0007829|PDB:2L5P"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:2L5P"
FT STRAND 118..126
FT /evidence="ECO:0007829|PDB:2L5P"
FT TURN 127..129
FT /evidence="ECO:0007829|PDB:2L5P"
FT STRAND 130..138
FT /evidence="ECO:0007829|PDB:2L5P"
FT STRAND 143..154
FT /evidence="ECO:0007829|PDB:2L5P"
FT HELIX 158..170
FT /evidence="ECO:0007829|PDB:2L5P"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:2L5P"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:2L5P"
SQ SEQUENCE 193 AA; 22222 MW; 29100E53BECDF772 CRC64;
MGPWWALWLI LTLPQILGGQ SPTMPQGFSQ MTSFQSNKFQ GEWFVLGLAD NTYKREHRPL
LHSFITLFKL RDNSEFQVTN SMTRGKHCST WSYTLIPTNK PGQFTRDNRG SGPGADKENI
QVIETDYVKF ALVLSLRQAS NQNITRVSLL GRDWKITHKT IDRFICLTKT QNLTKNNLLF
PDLTDWLLDP KVC
