ID   LC7L3_BOVIN             Reviewed;         432 AA.
AC   Q3SX41;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Luc7-like protein 3;
DE   AltName: Full=Cisplatin resistance-associated-overexpressed protein;
GN   Name=LUC7L3; Synonyms=CROP;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Ascending colon;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the Luc7 family. {ECO:0000305}.
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DR   EMBL; BC104519; AAI04520.1; -; mRNA.
DR   RefSeq; NP_001029856.1; NM_001034684.1.
DR   RefSeq; XP_005220659.1; XM_005220602.1.
DR   AlphaFoldDB; Q3SX41; -.
DR   SMR; Q3SX41; -.
DR   STRING; 9913.ENSBTAP00000002938; -.
DR   PaxDb; Q3SX41; -.
DR   PeptideAtlas; Q3SX41; -.
DR   PRIDE; Q3SX41; -.
DR   Ensembl; ENSBTAT00000002938; ENSBTAP00000002938; ENSBTAG00000002279.
DR   GeneID; 539955; -.
DR   KEGG; bta:539955; -.
DR   CTD; 51747; -.
DR   VEuPathDB; HostDB:ENSBTAG00000002279; -.
DR   VGNC; VGNC:31080; LUC7L3.
DR   eggNOG; KOG0796; Eukaryota.
DR   GeneTree; ENSGT00950000183213; -.
DR   HOGENOM; CLU_030397_0_1_1; -.
DR   InParanoid; Q3SX41; -.
DR   OrthoDB; 1499212at2759; -.
DR   TreeFam; TF354312; -.
DR   Proteomes; UP000009136; Chromosome 19.
DR   Bgee; ENSBTAG00000002279; Expressed in thymus and 106 other tissues.
DR   ExpressionAtlas; Q3SX41; baseline and differential.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
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   2: Evidence at transcript level;
KW   Acetylation; Coiled coil; DNA-binding; Isopeptide bond; mRNA processing;
KW   mRNA splicing; Nucleus; Phosphoprotein; Reference proteome;
KW   Ubl conjugation.
FT   CHAIN           1..432
FT                   /note="Luc7-like protein 3"
FT                   /id="PRO_0000233410"
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:0000250|UniProtKB:O95232"
FT   MOD_RES         425
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O95232"
FT   MOD_RES         431
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O95232"
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"
SQ   SEQUENCE   432 AA;  51496 MW;  525B55EC01372D11 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 ERRRSRSRDR RRSRSHDRSE RKHRSRSRDR RRSKSRDRKS
     YKHRSKSRDR EQDRKSKEKE KRGSDDKKSS VKSSSREKQS EDTNTESKES DTKNEVNGTS
     EDIKSEGDTQ SN