LANC2_MOUSE
ID LANC2_MOUSE Reviewed; 450 AA.
AC Q9JJK2;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=LanC-like protein 2;
DE AltName: Full=Testis-specific adriamycin sensitivity protein;
GN Name=Lancl2; Synonyms=Tasp;
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 [MRNA].
RA Sugimoto Y., Tsukahara S., Ishikawa E., Tsuruo T.;
RT "Isolation and identification of genes whose downregulation result in
RT anticancer drug resistance.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye, and Retina;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-198, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Spleen, and
RC 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: Necessary for abscisic acid (ABA) binding on the cell
CC membrane and activation of the ABA signaling pathway in granulocytes.
CC {ECO:0000250|UniProtKB:Q9NS86}.
CC -!- SUBUNIT: Interacts with an array of inositol phospholipids such as
CC phosphatidylinositol 3-phosphate (PI3P), phosphatidylinositol 4-
CC phosphate (PI4P) and phosphatidylinositol 5-phosphate (PI5P). PIP-
CC binding enhances membrane association. {ECO:0000250|UniProtKB:Q9NS86}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9NS86}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9NS86}. Cell membrane
CC {ECO:0000250|UniProtKB:Q9NS86}. Note=Localizes to the juxta-nuclear
CC vesicles. Associates with the cortical actin cytoskeleton. Cholesterol
CC depletion by methyl-beta-cyclodextrin causes partial dissociation from
CC the cell membrane in vitro and an enhanced cell detachment from the
CC matrix in vivo. {ECO:0000250|UniProtKB:Q9NS86}.
CC -!- PTM: Myristoylated. Essential for membrane association.
CC {ECO:0000250|UniProtKB:Q9NS86}.
CC -!- SIMILARITY: Belongs to the LanC-like protein family. {ECO:0000305}.
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DR EMBL; AB035967; BAA96801.1; -; mRNA.
DR EMBL; BC016072; AAH16072.1; -; mRNA.
DR CCDS; CCDS20185.1; -.
DR RefSeq; NP_598498.1; NM_133737.2.
DR AlphaFoldDB; Q9JJK2; -.
DR SMR; Q9JJK2; -.
DR BioGRID; 214964; 5.
DR IntAct; Q9JJK2; 2.
DR STRING; 10090.ENSMUSP00000052146; -.
DR ChEMBL; CHEMBL4802018; -.
DR iPTMnet; Q9JJK2; -.
DR PhosphoSitePlus; Q9JJK2; -.
DR SwissPalm; Q9JJK2; -.
DR EPD; Q9JJK2; -.
DR MaxQB; Q9JJK2; -.
DR PaxDb; Q9JJK2; -.
DR PRIDE; Q9JJK2; -.
DR ProteomicsDB; 290008; -.
DR Antibodypedia; 13819; 224 antibodies from 21 providers.
DR DNASU; 71835; -.
DR Ensembl; ENSMUST00000050077; ENSMUSP00000052146; ENSMUSG00000062190.
DR Ensembl; ENSMUST00000072954; ENSMUSP00000072723; ENSMUSG00000062190.
DR GeneID; 71835; -.
DR KEGG; mmu:71835; -.
DR UCSC; uc009ccn.2; mouse.
DR CTD; 55915; -.
DR MGI; MGI:1919085; Lancl2.
DR VEuPathDB; HostDB:ENSMUSG00000062190; -.
DR eggNOG; KOG2787; Eukaryota.
DR GeneTree; ENSGT00530000063186; -.
DR HOGENOM; CLU_036244_0_0_1; -.
DR InParanoid; Q9JJK2; -.
DR OMA; MAGTIHF; -.
DR OrthoDB; 681208at2759; -.
DR PhylomeDB; Q9JJK2; -.
DR TreeFam; TF300068; -.
DR BioGRID-ORCS; 71835; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Lancl2; mouse.
DR PRO; PR:Q9JJK2; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9JJK2; protein.
DR Bgee; ENSMUSG00000062190; Expressed in spermatocyte and 262 other tissues.
DR ExpressionAtlas; Q9JJK2; baseline and differential.
DR Genevisible; Q9JJK2; MM.
DR GO; GO:0030864; C:cortical actin cytoskeleton; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; ISO:MGI.
DR GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; ISO:MGI.
DR GO; GO:0010314; F:phosphatidylinositol-5-phosphate binding; ISO:MGI.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0009789; P:positive regulation of abscisic acid-activated signaling pathway; ISO:MGI.
DR Gene3D; 1.50.10.10; -; 1.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR007822; LANC-like.
DR InterPro; IPR020464; LanC-like_prot_euk.
DR Pfam; PF05147; LANC_like; 1.
DR PRINTS; PR01951; LANCEUKARYTE.
DR PRINTS; PR01950; LANCSUPER.
DR SMART; SM01260; LANC_like; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasm; Lipoprotein; Membrane; Myristate; Nucleus;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9NS86"
FT CHAIN 2..450
FT /note="LanC-like protein 2"
FT /id="PRO_0000191273"
FT REGION 2..14
FT /note="Interaction with inositol phospholipids"
FT /evidence="ECO:0000250"
FT MOD_RES 198
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 450 AA; 50777 MW; 854EF4684C34643F CRC64;
MGETMSKRLK FHLGEAEMEE RSFPNPFPDY EAAASAAGLA AGSAEETGRV CPLPTTEDPG
LPFHPNGKIV PNFIKRIQTK IKDLLQQMEE GLKTADPHDC SAYTGWTGIA LLYLQLYRVT
GDQTYLLRSL DYVKRTLRNL SGRRVTFLCG DAGPLAVGAV IYHKLKSECE SQECITKLLQ
MHRTIVCQES ELPDELLYGR AGYLYALLYL NTEIGPGTVG ETAIKEVVSA IIESGKSLSR
EERKSERCPL LYQWHRKQYV GAAHGMAGIY YMLMQPEAKV DQETLTEMVK PSIDYVRHKK
FRSGNYPSSL SNETDRLVHW CHGAPGVIHV LLQAYQVFKE EKYLKEAMEC SDVIWQRGLL
RKGYGICHGT SGNGYSFLSL YRLTQDKKYL YRACKFAEWC LDYGAHGCRI PDRPYSLFEG
MAGAVHFLSD ILVPETARFP AFELGFLQKD
