LCN5_MOUSE
ID LCN5_MOUSE Reviewed; 192 AA.
AC A2AJB7; O88787; Q3TS05; Q3UW42; Q9R2C6;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Epididymal-specific lipocalin-5;
DE AltName: Full=Epididymal retinoic acid-binding protein;
DE Short=E-RABP;
DE Short=mE-RABP;
DE AltName: Full=Epididymal secretory protein 10;
DE Short=MEP 10;
DE Contains:
DE RecName: Full=Epididymal-specific lipocalin-5, major form;
DE Contains:
DE RecName: Full=Epididymal-specific lipocalin-5, minor form;
DE Flags: Precursor;
GN Name=Lcn5 {ECO:0000312|MGI:MGI:1277241};
GN Synonyms=Mep10 {ECO:0000312|EMBL:AAD09351.1};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAC24316.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND INDUCTION.
RC STRAIN=SWR/J {ECO:0000269|PubMed:9607808};
RX PubMed=9607808; DOI=10.1210/endo.139.6.6074;
RA Lareyre J.-J., Zheng W.-L., Zhao G.-Q., Kasper S., Newcomer M.E.,
RA Matusik R.J., Ong D.E., Orgebin-Crist M.-C.;
RT "Molecular cloning and hormonal regulation of a murine epididymal retinoic
RT acid-binding protein messenger ribonucleic acid.";
RL Endocrinology 139:2971-2981(1998).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAD09351.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORM 1).
RC STRAIN=129 {ECO:0000312|EMBL:AAD09351.1};
RX PubMed=9669522;
RX DOI=10.1002/(sici)1098-2795(199808)50:4<387::aid-mrd2>3.0.co;2-e;
RA Lareyre J.-J., Mattei M.-G., Kasper S., Ong D.E., Matusik R.J.,
RA Orgebin-Crist M.-C.;
RT "Genomic organization and chromosomal localization of the murine epididymal
RT retinoic acid-binding protein (mE-RABP) gene.";
RL Mol. Reprod. Dev. 50:387-395(1998).
RN [3] {ECO:0000305, ECO:0000312|EMBL:BAE23077.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE23077.1};
RC TISSUE=Epididymis {ECO:0000312|EMBL:BAE23077.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5] {ECO:0000305}
RP PROTEIN SEQUENCE OF 27-39, FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=C57BL/6J {ECO:0000269|PubMed:1591332};
RX PubMed=1591332; DOI=10.1095/biolreprod46.5.747;
RA Rankin T.L., Tsuruta K.J., Holland M.K., Griswold M.D.,
RA Orgebin-Crist M.-C.;
RT "Isolation, immunolocalization, and sperm-association of three proteins of
RT 18, 25, and 29 kilodaltons secreted by the mouse epididymis.";
RL Biol. Reprod. 46:747-766(1992).
RN [6] {ECO:0000305}
RP SUBCELLULAR LOCATION.
RX PubMed=2393684; DOI=10.1095/biolreprod43.1.113;
RA Vreeburg J.T.M., Holland M.K., Cornwall G.A., Orgebin-Crist M.-C.;
RT "Secretion and transport of mouse epididymal proteins after injection of
RT 35S-methionine.";
RL Biol. Reprod. 43:113-120(1990).
RN [7] {ECO:0000305}
RP FUNCTION.
RX PubMed=1591333; DOI=10.1095/biolreprod46.5.767;
RA Rankin T.L., Ong D.E., Orgebin-Crist M.-C.;
RT "The 18-kDa mouse epididymal protein (MEP 10) binds retinoic acid.";
RL Biol. Reprod. 46:767-771(1992).
RN [8] {ECO:0000305}
RP TISSUE SPECIFICITY.
RX PubMed=14595821; DOI=10.1002/pmic.200300474;
RA Chaurand P., Fouchecourt S., DaGue B.B., Xu B.J., Reyzer M.L.,
RA Orgebin-Crist M.-C., Caprioli R.M.;
RT "Profiling and imaging proteins in the mouse epididymis by imaging mass
RT spectrometry.";
RL Proteomics 3:2221-2239(2003).
CC -!- FUNCTION: Associates with spermatozoa in the epididymal fluid but does
CC not bind tightly to them. Binds both all-trans and 13-cis retinoic
CC acid. May act as a retinoid carrier protein which is required for
CC epididymal function and/or sperm maturation.
CC {ECO:0000269|PubMed:1591332, ECO:0000269|PubMed:1591333}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1591332,
CC ECO:0000269|PubMed:2393684}. Note=Synthesized by the mid and distal
CC caput of the epididymis and secreted into the epididymal lumen.
CC {ECO:0000269|PubMed:1591332, ECO:0000269|PubMed:2393684}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1 {ECO:0000269|PubMed:9669522};
CC IsoId=A2AJB7-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:16141072};
CC IsoId=A2AJB7-2; Sequence=VSP_052839;
CC Name=3 {ECO:0000269|PubMed:16141072};
CC IsoId=A2AJB7-3; Sequence=VSP_052840;
CC Name=4 {ECO:0000269|PubMed:9607808};
CC IsoId=A2AJB7-4; Sequence=VSP_052838;
CC -!- TISSUE SPECIFICITY: Epididymal fluid of the caudal and corpus regions
CC (at protein level). {ECO:0000269|PubMed:14595821}.
CC -!- INDUCTION: Down-regulated to 11% of control levels 5 days after
CC castration and is not detectable by 20 days (at protein level). Levels
CC are partially restored by subsequent testosterone treatment.
CC {ECO:0000269|PubMed:9607808}.
CC -!- PTM: 2 different forms with differently processed N-termini exist.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD09351.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U68546; AAC24316.1; -; mRNA.
DR EMBL; U68381; AAD09351.1; ALT_INIT; Genomic_DNA.
DR EMBL; AK136629; BAE23077.1; -; mRNA.
DR EMBL; AK162355; BAE36871.1; -; mRNA.
DR EMBL; AL732590; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS38078.1; -. [A2AJB7-3]
DR CCDS; CCDS38079.1; -. [A2AJB7-1]
DR CCDS; CCDS71003.1; -. [A2AJB7-2]
DR RefSeq; NP_001036095.1; NM_001042630.2. [A2AJB7-3]
DR RefSeq; NP_001263186.1; NM_001276257.1. [A2AJB7-2]
DR RefSeq; NP_031973.2; NM_007947.3. [A2AJB7-1]
DR AlphaFoldDB; A2AJB7; -.
DR SMR; A2AJB7; -.
DR STRING; 10090.ENSMUSP00000028306; -.
DR PhosphoSitePlus; A2AJB7; -.
DR PaxDb; A2AJB7; -.
DR PRIDE; A2AJB7; -.
DR ProteomicsDB; 292241; -. [A2AJB7-1]
DR ProteomicsDB; 292242; -. [A2AJB7-2]
DR ProteomicsDB; 292243; -. [A2AJB7-3]
DR ProteomicsDB; 292244; -. [A2AJB7-4]
DR DNASU; 13863; -.
DR Ensembl; ENSMUST00000028306; ENSMUSP00000028306; ENSMUSG00000026937. [A2AJB7-1]
DR Ensembl; ENSMUST00000100312; ENSMUSP00000097887; ENSMUSG00000026937. [A2AJB7-2]
DR Ensembl; ENSMUST00000100313; ENSMUSP00000097888; ENSMUSG00000026937. [A2AJB7-3]
DR GeneID; 13863; -.
DR KEGG; mmu:13863; -.
DR UCSC; uc008itb.2; mouse. [A2AJB7-1]
DR UCSC; uc033hlx.1; mouse. [A2AJB7-2]
DR CTD; 13863; -.
DR MGI; MGI:1277241; Lcn5.
DR VEuPathDB; HostDB:ENSMUSG00000026937; -.
DR eggNOG; ENOG502TDU9; Eukaryota.
DR GeneTree; ENSGT01050000244868; -.
DR HOGENOM; CLU_1424476_0_0_1; -.
DR InParanoid; A2AJB7; -.
DR OMA; MENIMPF; -.
DR OrthoDB; 1291941at2759; -.
DR PhylomeDB; A2AJB7; -.
DR TreeFam; TF336103; -.
DR BioGRID-ORCS; 13863; 4 hits in 73 CRISPR screens.
DR PRO; PR:A2AJB7; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; A2AJB7; protein.
DR Bgee; ENSMUSG00000026937; Expressed in gonadal fat pad and 8 other tissues.
DR Genevisible; A2AJB7; MM.
DR GO; GO:0005615; C:extracellular space; TAS:MGI.
DR GO; GO:0005501; F:retinoid binding; TAS:MGI.
DR GO; GO:0036094; F:small molecule binding; IEA:InterPro.
DR GO; GO:0042573; P:retinoic acid metabolic process; TAS:MGI.
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 PANTHER; PTHR11430; PTHR11430; 1.
DR Pfam; PF00061; Lipocalin; 1.
DR SUPFAM; SSF50814; SSF50814; 1.
DR PROSITE; PS00213; LIPOCALIN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Direct protein sequencing; Disulfide bond;
KW Reference proteome; Secreted; Signal; Transport.
FT SIGNAL 1..26
FT /evidence="ECO:0000269|PubMed:1591332"
FT CHAIN 27..192
FT /note="Epididymal-specific lipocalin-5, major form"
FT /evidence="ECO:0000269|PubMed:1591332"
FT /id="PRO_0000339292"
FT CHAIN 30..192
FT /note="Epididymal-specific lipocalin-5, minor form"
FT /evidence="ECO:0000269|PubMed:1591332"
FT /id="PRO_0000339293"
FT DISULFID 89..183
FT /evidence="ECO:0000250|UniProtKB:P06911"
FT VAR_SEQ 1..29
FT /note="MCSVARHMESIMLFTLLGLCVGLAAGTEA -> M (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:9607808"
FT /id="VSP_052838"
FT VAR_SEQ 181..192
FT /note="LTCVNALQSGQI -> YIEIKALPKPGS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_052839"
FT VAR_SEQ 181..192
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_052840"
SQ SEQUENCE 192 AA; 21013 MW; E91DA019DEF21F5B CRC64;
MCSVARHMES IMLFTLLGLC VGLAAGTEAA VVKDFDVNKF LGFWYEIALA SKMGAYGLAH
KEEKMGAMVV ELKENLLALT TTYYNEGHCV LEKVAATQVD GSAKYKVTRI SGEKEVVVVA
TDYMTYTVID ITSLVAGAVH RAMKLYSRSL DNNGEALNNF QKIALKHGFS ETDIHILKHD
LTCVNALQSG QI
