DLK2_MOUSE
ID DLK2_MOUSE Reviewed; 382 AA.
AC Q8K1E3; B5B9L4; Q0IIP7; Q148N7; Q9QYP3;
DT 25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 3.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Protein delta homolog 2;
DE Short=DLK-2;
DE AltName: Full=Endothelial cell-specific protein S-1;
DE AltName: Full=Epidermal growth factor-like protein 9;
DE Short=EGF-like protein 9;
DE Flags: Precursor;
GN Name=Dlk2; Synonyms=Egfl9;
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] (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=17320102; DOI=10.1016/j.jmb.2006.10.020;
RA Nueda M.L., Baladron V., Garcia-Ramirez J.J., Sanchez-Solana B.,
RA Ruvira M.D., Rivero S., Ballesteros M.A., Monsalve E.M., Diaz-Guerra M.J.,
RA Ruiz-Hidalgo M.J., Laborda J.;
RT "The novel gene EGFL9/Dlk2, highly homologous to Dlk1, functions as a
RT modulator of adipogenesis.";
RL J. Mol. Biol. 367:1270-1280(2007).
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 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=FVB/N; TISSUE=Salivary gland;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-65 (ISOFORM 1).
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 259-382.
RA Fukudome K., Tsuneyoshi N., Kimoto M.;
RT "Endothelial cell specific protein S-1.";
RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Regulates adipogenesis. {ECO:0000269|PubMed:17320102}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=2;
CC IsoId=Q8K1E3-1; Sequence=Displayed;
CC Name=1;
CC IsoId=Q8K1E3-3; Sequence=VSP_039583;
CC Name=3;
CC IsoId=Q8K1E3-4; Sequence=VSP_039584;
CC -!- TISSUE SPECIFICITY: Detected in a number of tissues including lung,
CC brain, adrenal gland, testis, adult liver, placenta, ovary and thymus.
CC Not detected in fetal liver or in adult spleen, muscle and heart.
CC {ECO:0000269|PubMed:17320102}.
CC -!- DEVELOPMENTAL STAGE: Absent from liver after birth, but increases
CC around postnatal day 16. {ECO:0000269|PubMed:17320102}.
CC -!- MISCELLANEOUS: [Isoform 3]: Splice sites are non-canonical.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA88686.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; FM180474; CAQ86598.1; -; mRNA.
DR EMBL; CT009572; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466559; EDL23496.1; -; Genomic_DNA.
DR EMBL; BC019431; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC118057; AAI18058.1; -; mRNA.
DR EMBL; BC122518; AAI22519.1; -; mRNA.
DR EMBL; BY271273; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AB011019; BAA88686.1; ALT_INIT; mRNA.
DR CCDS; CCDS37634.2; -. [Q8K1E3-1]
DR RefSeq; NP_001272942.1; NM_001286013.1. [Q8K1E3-1]
DR RefSeq; NP_001272957.1; NM_001286028.1. [Q8K1E3-1]
DR RefSeq; XP_006523451.1; XM_006523388.1. [Q8K1E3-1]
DR RefSeq; XP_006523452.1; XM_006523389.1. [Q8K1E3-1]
DR RefSeq; XP_011244537.1; XM_011246235.1.
DR AlphaFoldDB; Q8K1E3; -.
DR SMR; Q8K1E3; -.
DR STRING; 10090.ENSMUSP00000058470; -.
DR GlyGen; Q8K1E3; 1 site.
DR iPTMnet; Q8K1E3; -.
DR PhosphoSitePlus; Q8K1E3; -.
DR PaxDb; Q8K1E3; -.
DR PRIDE; Q8K1E3; -.
DR ProteomicsDB; 279684; -. [Q8K1E3-1]
DR ProteomicsDB; 279685; -. [Q8K1E3-3]
DR ProteomicsDB; 279686; -. [Q8K1E3-4]
DR Antibodypedia; 30417; 122 antibodies from 24 providers.
DR DNASU; 106565; -.
DR Ensembl; ENSMUST00000061722; ENSMUSP00000058470; ENSMUSG00000047428. [Q8K1E3-3]
DR Ensembl; ENSMUST00000166280; ENSMUSP00000126993; ENSMUSG00000047428. [Q8K1E3-1]
DR Ensembl; ENSMUST00000166617; ENSMUSP00000128897; ENSMUSG00000047428. [Q8K1E3-1]
DR GeneID; 106565; -.
DR KEGG; mmu:106565; -.
DR UCSC; uc008csl.2; mouse. [Q8K1E3-1]
DR CTD; 65989; -.
DR MGI; MGI:2146838; Dlk2.
DR VEuPathDB; HostDB:ENSMUSG00000047428; -.
DR eggNOG; KOG1217; Eukaryota.
DR GeneTree; ENSGT00940000160761; -.
DR HOGENOM; CLU_039179_1_0_1; -.
DR InParanoid; Q8K1E3; -.
DR OMA; QECQVGM; -.
DR OrthoDB; 880666at2759; -.
DR TreeFam; TF351835; -.
DR BioGRID-ORCS; 106565; 0 hits in 74 CRISPR screens.
DR ChiTaRS; Dlk2; mouse.
DR PRO; PR:Q8K1E3; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q8K1E3; protein.
DR Bgee; ENSMUSG00000047428; Expressed in embryonic brain and 100 other tissues.
DR ExpressionAtlas; Q8K1E3; baseline and differential.
DR Genevisible; Q8K1E3; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0005112; F:Notch binding; IBA:GO_Central.
DR GO; GO:0045746; P:negative regulation of Notch signaling pathway; IGI:MGI.
DR GO; GO:0045598; P:regulation of fat cell differentiation; IDA:UniProtKB.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR013032; EGF-like_CS.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR Pfam; PF00008; EGF; 3.
DR Pfam; PF12661; hEGF; 1.
DR SMART; SM00181; EGF; 6.
DR SMART; SM00179; EGF_CA; 4.
DR PROSITE; PS00010; ASX_HYDROXYL; 2.
DR PROSITE; PS00022; EGF_1; 6.
DR PROSITE; PS01186; EGF_2; 6.
DR PROSITE; PS50026; EGF_3; 6.
DR PROSITE; PS01187; EGF_CA; 2.
PE 2: Evidence at transcript level;
KW Alternative splicing; Calcium; Disulfide bond; EGF-like domain;
KW Glycoprotein; Membrane; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..382
FT /note="Protein delta homolog 2"
FT /id="PRO_0000396620"
FT TOPO_DOM 27..305
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 306..326
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 327..382
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 27..58
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 62..89
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 91..129
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 131..172
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 174..210
FT /note="EGF-like 5; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 212..248
FT /note="EGF-like 6; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 29..40
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 33..46
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 48..57
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 66..71
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 79..88
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 95..107
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 101..117
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 119..128
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 135..148
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 142..160
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 162..171
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 178..189
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 183..198
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 200..209
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 216..227
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 221..236
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 238..247
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT VAR_SEQ 1
FT /note="M -> MKITMRVSVPLSPRQAASQPVPSHRCLHVWPFIRPSLLRPELTM
FT (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_039583"
FT VAR_SEQ 1
FT /note="M -> MKITMRPGDASPPSRRCLHVWPFIRPSLLRPELTM (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_039584"
FT CONFLICT 236
FT /note="C -> Y (in Ref. 4; AAI18058)"
FT /evidence="ECO:0000305"
FT CONFLICT 295..311
FT /note="Missing (in Ref. 6; BAA88686)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 382 AA; 40404 MW; F2C82AD649CA0B3C CRC64;
MPSGCRCLNL VCLLCILGAT SQPARADDCS SHCDLAHGCC APDGSCRCDP GWEGLHCERC
VRMPGCQHGT CHQPWQCICH SGWAGKFCDK DEHICTSQSP CQNGGQCVYD GGGEYHCVCL
PGFHGRGCER KAGPCEQAGF PCRNGGQCQD NQGFALNFTC RCLAGFMGAH CEVNVDDCLM
RPCANGATCI DGINRFSCLC PEGFAGRFCT INLDDCASRP CQRGARCRDR VHDFDCLCPS
GYGGKTCELV LPAPEPASVG TPQMPTSAVV VPATGPAPHS AGAGLLRISV KEVVRRQESG
LGESSLVALV VFGSLTAALV LATVLLTLRA WRRGICPTGP CCYPAPHYAP ARQDQECQVS
MLPAGFPLSP DLPPEPGKTT AL
