LC7L3_MOUSE
ID LC7L3_MOUSE Reviewed; 432 AA.
AC Q5SUF2; Q3U9D5; Q8BUJ5; Q921Z3; Q9CRS7; Q9CTY4;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Luc7-like protein 3;
DE AltName: Full=Cisplatin resistance-associated-overexpressed protein;
GN Name=Luc7l3; Synonyms=Crop;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-252 (ISOFORMS 1/2/3), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 165-432 (ISOFORM 1).
RC STRAIN=C57BL/6J;
RC TISSUE=Embryonic head, Embryonic heart, Macrophage, and Placenta;
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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-425 AND SER-431, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-420; SER-425 AND SER-431, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Binds cAMP regulatory element DNA sequence. May play a role
CC in RNA splicing (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: May interact with SFRS1 and form homodimers. Interacts with
CC JMJD6. Interacts with RBM25. Interacts with RSRC1 (via Arg/Ser-rich
CC domain). Interacts with RRP1B. {ECO:0000250|UniProtKB:O95232}.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q5SUF2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5SUF2-2; Sequence=VSP_018138;
CC Name=3;
CC IsoId=Q5SUF2-3; Sequence=VSP_018139;
CC -!- SIMILARITY: Belongs to the Luc7 family. {ECO:0000305}.
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DR EMBL; AK014362; BAB29297.1; -; mRNA.
DR EMBL; AK019464; BAB31736.1; -; mRNA.
DR EMBL; AK084714; BAC39261.1; -; mRNA.
DR EMBL; AK151228; BAE30220.1; -; mRNA.
DR EMBL; AK151839; BAE30732.1; -; mRNA.
DR EMBL; AL645846; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL645965; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC009092; AAH09092.1; -; mRNA.
DR CCDS; CCDS25252.1; -. [Q5SUF2-2]
DR CCDS; CCDS88223.1; -. [Q5SUF2-1]
DR CCDS; CCDS88224.1; -. [Q5SUF2-3]
DR RefSeq; NP_080589.1; NM_026313.1. [Q5SUF2-2]
DR RefSeq; XP_006534073.1; XM_006534010.3.
DR RefSeq; XP_006534074.1; XM_006534011.3.
DR AlphaFoldDB; Q5SUF2; -.
DR SMR; Q5SUF2; -.
DR BioGRID; 212365; 3.
DR IntAct; Q5SUF2; 2.
DR STRING; 10090.ENSMUSP00000021226; -.
DR iPTMnet; Q5SUF2; -.
DR PhosphoSitePlus; Q5SUF2; -.
DR SwissPalm; Q5SUF2; -.
DR EPD; Q5SUF2; -.
DR MaxQB; Q5SUF2; -.
DR PaxDb; Q5SUF2; -.
DR PeptideAtlas; Q5SUF2; -.
DR PRIDE; Q5SUF2; -.
DR ProteomicsDB; 252459; -. [Q5SUF2-1]
DR ProteomicsDB; 252460; -. [Q5SUF2-2]
DR ProteomicsDB; 252461; -. [Q5SUF2-3]
DR Antibodypedia; 18160; 101 antibodies from 24 providers.
DR DNASU; 67684; -.
DR Ensembl; ENSMUST00000021226; ENSMUSP00000021226; ENSMUSG00000020863. [Q5SUF2-2]
DR Ensembl; ENSMUST00000107820; ENSMUSP00000103450; ENSMUSG00000020863. [Q5SUF2-1]
DR Ensembl; ENSMUST00000107821; ENSMUSP00000103451; ENSMUSG00000020863. [Q5SUF2-1]
DR Ensembl; ENSMUST00000166312; ENSMUSP00000129919; ENSMUSG00000020863. [Q5SUF2-3]
DR GeneID; 67684; -.
DR KEGG; mmu:67684; -.
DR UCSC; uc007kyh.1; mouse. [Q5SUF2-2]
DR UCSC; uc007kyi.1; mouse. [Q5SUF2-1]
DR UCSC; uc007kyj.1; mouse. [Q5SUF2-3]
DR CTD; 51747; -.
DR MGI; MGI:1914934; Luc7l3.
DR VEuPathDB; HostDB:ENSMUSG00000020863; -.
DR eggNOG; KOG0796; Eukaryota.
DR GeneTree; ENSGT00950000183213; -.
DR HOGENOM; CLU_030397_0_1_1; -.
DR InParanoid; Q5SUF2; -.
DR OMA; DNSHYNQ; -.
DR OrthoDB; 1499212at2759; -.
DR PhylomeDB; Q5SUF2; -.
DR TreeFam; TF354312; -.
DR BioGRID-ORCS; 67684; 24 hits in 60 CRISPR screens.
DR ChiTaRS; Luc7l3; mouse.
DR PRO; PR:Q5SUF2; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q5SUF2; protein.
DR Bgee; ENSMUSG00000020863; Expressed in metanephric cortical collecting duct and 260 other tissues.
DR ExpressionAtlas; Q5SUF2; baseline and differential.
DR Genevisible; Q5SUF2; MM.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005685; C:U1 snRNP; IBA:GO_Central.
DR GO; GO:0071004; C:U2-type prespliceosome; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
DR GO; GO:0006376; P:mRNA splice site selection; IBA:GO_Central.
DR GO; GO:0008380; P:RNA splicing; ISS:UniProtKB.
DR InterPro; IPR004882; Luc7-rel.
DR PANTHER; PTHR12375; PTHR12375; 1.
DR Pfam; PF03194; LUC7; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; DNA-binding;
KW Isopeptide bond; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..432
FT /note="Luc7-like protein 3"
FT /id="PRO_0000233411"
FT REGION 234..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 124..181
FT /evidence="ECO:0000255"
FT COMPBIAS 234..287
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..363
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..422
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:O95232"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95232"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95232"
FT MOD_RES 115
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95232"
FT MOD_RES 231
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O95232"
FT MOD_RES 420
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 425
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 431
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT CROSSLNK 424
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:O95232"
FT CROSSLNK 424
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:O95232"
FT VAR_SEQ 427..432
FT /note="GDTQSN -> VQRKYAQMKMELSRVRRHTKASSEGKDSVVLQNILRYIVLSQ
FT LFCSRLRAPISVPLWKLLSTYVI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_018138"
FT VAR_SEQ 427..432
FT /note="GDTQSN -> VQRKYAQMKMELSRVRRHTKASSEGKDSVVLQNILRTTVEEF
FT LKNTENGIK (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_018139"
FT CONFLICT 402
FT /note="D -> E (in Ref. 1; BAC39261)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 432 AA; 51450 MW; 2546F0AE9A0CC160 CRC64;
MISAAQLLDE LMGRDRNLAP DEKRSNVRWD HESVCKYYLC GFCPAELFTN TRSDLGPCEK
IHDENLRKQY EKSSRFMKVG YERDFLRYLQ SLLAEVERRI RRGHARLALS QNQQSSGAAG
PTGKNEEKIQ VLTDKIDVLL QQIEELGSEG KVEEAQGMMK LVEQLKEERE LLRSTTSTIE
SFAAQEKQME VCEVCGAFLI VGDAQSRVDD HLMGKQHMGY AKIKATVEEL KEKLRKRTEE
PDRDERLKKE KQEREEREKE REREREERER KRRREEEERE KERARDRERR KRSRSRSRHS
SRTSDRRCSR SRDHKRSRSR DRRRSRSRDR RRSRSHDRSE RKHRSRSRDR RRSKSRDRKS
YKHRSKSRDR EQDRKSKEKE KKGSDDKKSS VKSSSREKQS EDTNPESKES DTKNEVNGTS
EDIKSEGDTQ SN
