LTV1_MOUSE
ID LTV1_MOUSE Reviewed; 470 AA.
AC Q6NSQ7; Q9D0F5;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Protein LTV1 homolog;
GN Name=Ltv1;
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].
RC STRAIN=C57BL/6J;
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 MRNA].
RC STRAIN=C57BL/6J, and Czech II; TISSUE=Eye, and 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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
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 -!- SIMILARITY: Belongs to the LTV1 family. {ECO:0000305}.
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DR EMBL; AK011491; BAB27653.1; -; mRNA.
DR EMBL; BC067062; AAH67062.1; -; mRNA.
DR EMBL; BC069962; AAH69962.1; -; mRNA.
DR CCDS; CCDS35845.1; -.
DR RefSeq; NP_852135.1; NM_181470.4.
DR AlphaFoldDB; Q6NSQ7; -.
DR SMR; Q6NSQ7; -.
DR BioGRID; 237279; 1.
DR IntAct; Q6NSQ7; 3.
DR MINT; Q6NSQ7; -.
DR STRING; 10090.ENSMUSP00000019950; -.
DR iPTMnet; Q6NSQ7; -.
DR PhosphoSitePlus; Q6NSQ7; -.
DR EPD; Q6NSQ7; -.
DR MaxQB; Q6NSQ7; -.
DR PaxDb; Q6NSQ7; -.
DR PeptideAtlas; Q6NSQ7; -.
DR PRIDE; Q6NSQ7; -.
DR ProteomicsDB; 293412; -.
DR Ensembl; ENSMUST00000019950; ENSMUSP00000019950; ENSMUSG00000019814.
DR GeneID; 353258; -.
DR KEGG; mmu:353258; -.
DR UCSC; uc007ekp.1; mouse.
DR CTD; 84946; -.
DR MGI; MGI:2447810; Ltv1.
DR VEuPathDB; HostDB:ENSMUSG00000019814; -.
DR eggNOG; KOG2637; Eukaryota.
DR GeneTree; ENSGT00390000002789; -.
DR HOGENOM; CLU_035718_0_0_1; -.
DR InParanoid; Q6NSQ7; -.
DR OMA; HPVVMQC; -.
DR OrthoDB; 917248at2759; -.
DR PhylomeDB; Q6NSQ7; -.
DR TreeFam; TF314845; -.
DR Reactome; R-MMU-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR BioGRID-ORCS; 353258; 24 hits in 73 CRISPR screens.
DR PRO; PR:Q6NSQ7; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q6NSQ7; protein.
DR Bgee; ENSMUSG00000019814; Expressed in umbilical cord and 281 other tissues.
DR Genevisible; Q6NSQ7; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0030688; C:preribosome, small subunit precursor; IBA:GO_Central.
DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IBA:GO_Central.
DR GO; GO:0000056; P:ribosomal small subunit export from nucleus; IBA:GO_Central.
DR InterPro; IPR007307; Ltv1.
DR PANTHER; PTHR21531; PTHR21531; 1.
DR Pfam; PF04180; LTV; 2.
PE 1: Evidence at protein level;
KW Coiled coil; Phosphoprotein; Reference proteome.
FT CHAIN 1..470
FT /note="Protein LTV1 homolog"
FT /id="PRO_0000302814"
FT REGION 25..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 400..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 414..470
FT /evidence="ECO:0000255"
FT COMPBIAS 176..196
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..437
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96GA3"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96GA3"
FT MOD_RES 243
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 326
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96GA3"
FT MOD_RES 403
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96GA3"
FT CONFLICT 86
FT /note="S -> T (in Ref. 2; AAH69962)"
FT /evidence="ECO:0000305"
FT CONFLICT 185
FT /note="H -> N (in Ref. 2; AAH69962)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 470 AA; 54023 MW; 178DE2294FE69895 CRC64;
MPHRKKKPFI EKKKAVSFHL VHRSQRDPLA ADETAPQRVL LPTQKVNDEE RRAEQRKYGV
FFDDDYDYLQ HLKEPSGPAE LIPSTSFATP LCDKTEDPCV YSSTGIKLPS SVFASEFEED
VGLLNKAAPV SGPRLDFDPD IVAALDDDFD FDDPENLLED DFILQANKPT GGERMDTESE
EDDGHEWEDM DDEEGSDDRS SAGFLSDGGD LSAPGSPQEA MKKHLFWEEE TKSRFTEYSM
TSSVMRRNEQ LTLHDERFEK FYEQYDDVEI GALDNAELEG TIQVDSNRLQ EVLNDYYKEK
AENCVKLSTL EPFEDQDLPT NELDESEKEE TITVVLEEAK EKWDCESICS TYSNLYNHPQ
LIKYEPKPKQ IHLSSKTGIP LNVLPKKGLT AKQVERMQMI NGSDLPKVST QPRSKDETKE
DKRARKQAIK EERKERRVEK KANKLAFKLE KRRQEKELLN LKKNIEGLKL
