B2L13_MOUSE
ID B2L13_MOUSE Reviewed; 434 AA.
AC P59017; Q543S1;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Bcl-2-like protein 13;
DE Short=Bcl2-L-13;
DE AltName: Full=Bcl-rambo;
DE AltName: Full=Protein Mil1;
GN Name=Bcl2l13; Synonyms=Mil1;
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; TISSUE=Cerebellum, Liver, and Testis;
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].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; 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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-387, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17208939; DOI=10.1074/mcp.m600218-mcp200;
RA Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
RT "Mitochondrial phosphoproteome revealed by an improved IMAC method and
RT MS/MS/MS.";
RL Mol. Cell. Proteomics 6:669-676(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-343, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-343 AND SER-347, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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: May promote the activation of caspase-3 and apoptosis.
CC -!- SUBUNIT: Monomer. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000250}; Single-pass
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Bcl-2 family. {ECO:0000305}.
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DR EMBL; AK047223; BAC32999.1; -; mRNA.
DR EMBL; AK132774; BAE21351.1; -; mRNA.
DR EMBL; AK168833; BAE40657.1; -; mRNA.
DR EMBL; CH466523; EDK99647.1; -; Genomic_DNA.
DR EMBL; BC027307; AAH27307.1; -; mRNA.
DR EMBL; BC029016; AAH29016.1; -; mRNA.
DR CCDS; CCDS20485.1; -.
DR RefSeq; NP_705736.1; NM_153516.2.
DR AlphaFoldDB; P59017; -.
DR BioGRID; 220423; 1.
DR IntAct; P59017; 1.
DR STRING; 10090.ENSMUSP00000009256; -.
DR iPTMnet; P59017; -.
DR PhosphoSitePlus; P59017; -.
DR SwissPalm; P59017; -.
DR EPD; P59017; -.
DR jPOST; P59017; -.
DR MaxQB; P59017; -.
DR PaxDb; P59017; -.
DR PeptideAtlas; P59017; -.
DR PRIDE; P59017; -.
DR ProteomicsDB; 273455; -.
DR TopDownProteomics; P59017; -.
DR Antibodypedia; 3673; 275 antibodies from 35 providers.
DR DNASU; 94044; -.
DR Ensembl; ENSMUST00000009256; ENSMUSP00000009256; ENSMUSG00000009112.
DR GeneID; 94044; -.
DR KEGG; mmu:94044; -.
DR UCSC; uc009dnt.1; mouse.
DR CTD; 23786; -.
DR MGI; MGI:2136959; Bcl2l13.
DR VEuPathDB; HostDB:ENSMUSG00000009112; -.
DR eggNOG; ENOG502R6AP; Eukaryota.
DR GeneTree; ENSGT00390000015552; -.
DR HOGENOM; CLU_032647_0_0_1; -.
DR InParanoid; P59017; -.
DR OMA; HDQISPP; -.
DR OrthoDB; 977051at2759; -.
DR PhylomeDB; P59017; -.
DR TreeFam; TF330744; -.
DR BioGRID-ORCS; 94044; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Bcl2l13; mouse.
DR PRO; PR:P59017; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; P59017; protein.
DR Bgee; ENSMUSG00000009112; Expressed in substantia propria of cornea and 260 other tissues.
DR ExpressionAtlas; P59017; baseline and differential.
DR Genevisible; P59017; MM.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
DR Gene3D; 1.10.437.10; -; 1.
DR InterPro; IPR036834; Bcl-2-like_sf.
DR InterPro; IPR046371; Bcl-2_BH1-3.
DR InterPro; IPR002475; Bcl2-like.
DR InterPro; IPR042398; BCL2L13.
DR PANTHER; PTHR15758; PTHR15758; 1.
DR Pfam; PF00452; Bcl-2; 1.
DR SUPFAM; SSF56854; SSF56854; 1.
DR PROSITE; PS50062; BCL2_FAMILY; 1.
PE 1: Evidence at protein level;
KW Apoptosis; Membrane; Mitochondrion; Phosphoprotein; Reference proteome;
KW Repeat; Transmembrane; Transmembrane helix.
FT CHAIN 1..434
FT /note="Bcl-2-like protein 13"
FT /id="PRO_0000143074"
FT TRANSMEM 409..429
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 243..253
FT /note="A"
FT REPEAT 258..268
FT /note="A; approximate"
FT REGION 224..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 282..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 363..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 14..30
FT /note="BH4"
FT MOTIF 97..113
FT /note="BH3"
FT MOTIF 144..154
FT /note="BH1"
FT MOTIF 190..203
FT /note="BH2"
FT COMPBIAS 372..392
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXK5"
FT MOD_RES 256
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXK5"
FT MOD_RES 258
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXK5"
FT MOD_RES 300
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXK5"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 347
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 377
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXK5"
FT MOD_RES 387
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17208939"
FT CONFLICT 8
FT /note="S -> P (in Ref. 3; AAH27307)"
FT /evidence="ECO:0000305"
FT CONFLICT 66
FT /note="T -> A (in Ref. 3; AAH27307)"
FT /evidence="ECO:0000305"
FT CONFLICT 326
FT /note="T -> A (in Ref. 3; AAH27307)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 434 AA; 46719 MW; E84790F7CBCE9B67 CRC64;
MASSTTASLG FHYETKYVVL SYLGLLSQEK QQGPSPPGVQ LDVAPQSLNP EVLLKLKSEI
EEELKTLDKE VSEAFTSTGF DCHTSPVFSP ANPESSIEDC LAHLGERVSQ DLKEPLQKAL
QTILSQPVTY EAYRECTVET AVHASGWNKL LVPLVLLQHL LLELTRRGQE PLRMLLQFGV
MYLEEHAAEF IIQQGGWGSV FSLEPEEEEY PGIIAEDSND IYILPSDNSG QVSPPESPTV
TTSWQSESLP VSLSASQSWH TESLPVSLGP ESWQQIAMDP EEVKSLDSSG AGEKSENNSS
NSDIVHVEKE EVPEEAFPGA AAPLLTQVPT VEAPEMMRAE KTSPTPSVFV ELGEEELEAV
TARPEAVERA EGAAQLSEER AGSRKKSHTG EAAAVRGAKS GLPAEGKAVL LFGGAAAVAI
LAVAVGVALA LRRK
