DLK1_MOUSE
ID DLK1_MOUSE Reviewed; 385 AA.
AC Q09163; Q07645; Q62208;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 177.
DE RecName: Full=Protein delta homolog 1;
DE Short=DLK-1;
DE AltName: Full=Adipocyte differentiation inhibitor protein;
DE AltName: Full=Preadipocyte factor 1;
DE Short=Pref-1;
DE Contains:
DE RecName: Full=Fetal antigen 1;
DE Short=FA1;
DE Flags: Precursor;
GN Name=Dlk1; Synonyms=Dlk, Pref1, Scp-1;
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], AND FUNCTION.
RC STRAIN=SWR/J; TISSUE=Fibroblast;
RX PubMed=8095043; DOI=10.1016/s0021-9258(18)53544-4;
RA Laborda J., Sausville E.A., Hoffman T., Notario V.;
RT "dlk, a putative mammalian homeotic gene differentially expressed in small
RT cell lung carcinoma and neuroendocrine tumor cell line.";
RL J. Biol. Chem. 268:3817-3820(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=8500166; DOI=10.1016/0092-8674(93)90252-l;
RA Smas C.M., Sul H.S.;
RT "Pref-1, a protein containing EGF-like repeats, inhibits adipocyte
RT differentiation.";
RL Cell 73:725-734(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT LYS-347 DEL.
RC TISSUE=Adrenal gland, and Placenta;
RX PubMed=7711066; DOI=10.1016/0167-4781(95)00007-4;
RA Lee Y.L., Helman L., Hoffman T., Laborda J.;
RT "dlk, pG2 and Pref-1 mRNAs encode similar proteins belonging to the EGF-
RT like superfamily. Identification of polymorphic variants of this RNA.";
RL Biochim. Biophys. Acta 1261:223-232(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Maruyama K., Nishijima S., Kuromitsu S., Ichikawa A., Masuda E.,
RA Takemoto T., Kodama H., Kawashima H.;
RL Submitted (AUG-1993) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-8, AND ALTERNATIVE SPLICING.
RX PubMed=7519443; DOI=10.1021/bi00197a029;
RA Smas C.M., Green D., Sul H.S.;
RT "Structural characterization and alternate splicing of the gene encoding
RT the preadipocyte EGF-like protein pref-1.";
RL Biochemistry 33:9257-9265(1994).
RN [6]
RP GLYCOSYLATION AT SER-94; ASN-100; ASN-165; ASN-174; SER-216; THR-224;
RP THR-258; THR-267 AND THR-271, AND STRUCTURE OF CARBOHYDRATE.
RX PubMed=9118998; DOI=10.1111/j.1432-1033.1997.00334.x;
RA Krogh T.N., Bachmann E., Teisner B., Skjoedt K., Hoejrup P.;
RT "Glycosylation analysis and protein structure determination of murine fetal
RT antigen 1 (mFA1) -- the circulating gene product of the delta-like protein
RT (dlk), preadipocyte factor 1 (Pref-1) and stromal-cell-derived protein 1
RT (SCP-1) cDNAs.";
RL Eur. J. Biochem. 244:334-342(1997).
RN [7]
RP TISSUE SPECIFICITY, AND 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).
CC -!- FUNCTION: May have a role in neuroendocrine differentiation. Inhibits
CC adipocyte differentiation. {ECO:0000269|PubMed:8095043,
CC ECO:0000269|PubMed:8500166}.
CC -!- SUBUNIT: Monomer. Interacts with SH3RF2 (By similarity).
CC {ECO:0000250|UniProtKB:O70534}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC Cytoplasm {ECO:0000250|UniProtKB:O70534}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Comment=Additional isoforms seem to exist.;
CC Name=A;
CC IsoId=Q09163-1; Sequence=Displayed;
CC Name=B;
CC IsoId=Q09163-2; Sequence=VSP_001380;
CC Name=C;
CC IsoId=Q09163-3; Sequence=VSP_001381;
CC Name=C2;
CC IsoId=Q09163-4; Sequence=VSP_001382;
CC Name=D;
CC IsoId=Q09163-5; Sequence=VSP_001378;
CC Name=D2;
CC IsoId=Q09163-6; Sequence=VSP_001379;
CC -!- TISSUE SPECIFICITY: Highly expressed in fetal liver, placenta, adult
CC adrenal gland, brain, testis and ovary and, to a lesser degree, in
CC adult kidney, muscle, thymus and heart. {ECO:0000269|PubMed:17320102}.
CC -!- DEVELOPMENTAL STAGE: Expression is elevated in liver after birth but
CC starts to decline around postnatal day 16.
CC {ECO:0000269|PubMed:17320102}.
CC -!- PTM: N- and O-glycosylated. {ECO:0000269|PubMed:9118998}.
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DR EMBL; Z12171; CAA78162.1; -; mRNA.
DR EMBL; U15980; AAB60495.1; -; mRNA.
DR EMBL; L12721; AAA37175.1; -; mRNA.
DR EMBL; S71340; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; D16847; BAA04121.1; -; mRNA.
DR CCDS; CCDS26168.1; -. [Q09163-1]
DR CCDS; CCDS49173.1; -. [Q09163-6]
DR CCDS; CCDS49174.1; -. [Q09163-2]
DR CCDS; CCDS56863.1; -. [Q09163-3]
DR PIR; A54785; A54785.
DR PIR; S53718; S53718.
DR RefSeq; NP_034182.2; NM_010052.5.
DR AlphaFoldDB; Q09163; -.
DR SMR; Q09163; -.
DR BioGRID; 199231; 1.
DR DIP; DIP-6010N; -.
DR IntAct; Q09163; 1.
DR STRING; 10090.ENSMUSP00000105470; -.
DR GlyConnect; 153; 9 N-Linked glycans (1 site), 4 O-Linked glycans (3 sites).
DR GlyGen; Q09163; 11 sites, 18 N-linked glycans (3 sites), 6 O-linked glycans (7 sites).
DR iPTMnet; Q09163; -.
DR PhosphoSitePlus; Q09163; -.
DR jPOST; Q09163; -.
DR PaxDb; Q09163; -.
DR PRIDE; Q09163; -.
DR ProteomicsDB; 279427; -. [Q09163-1]
DR ProteomicsDB; 279428; -. [Q09163-2]
DR ProteomicsDB; 279429; -. [Q09163-3]
DR ProteomicsDB; 279430; -. [Q09163-4]
DR ProteomicsDB; 279431; -. [Q09163-5]
DR ProteomicsDB; 279432; -. [Q09163-6]
DR DNASU; 13386; -.
DR GeneID; 13386; -.
DR KEGG; mmu:13386; -.
DR CTD; 8788; -.
DR MGI; MGI:94900; Dlk1.
DR eggNOG; KOG1217; Eukaryota.
DR InParanoid; Q09163; -.
DR OrthoDB; 619882at2759; -.
DR PhylomeDB; Q09163; -.
DR BioGRID-ORCS; 13386; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Dlk1; mouse.
DR PRO; PR:Q09163; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q09163; protein.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0030282; P:bone mineralization; IMP:MGI.
DR GO; GO:0030154; P:cell differentiation; ISO:MGI.
DR GO; GO:0048706; P:embryonic skeletal system development; IDA:MGI.
DR GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR GO; GO:0045599; P:negative regulation of fat cell differentiation; IDA:HGNC.
DR GO; GO:0045746; P:negative regulation of Notch signaling pathway; IGI:MGI.
DR GO; GO:0030279; P:negative regulation of ossification; ISO:MGI.
DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; ISO:MGI.
DR GO; GO:1905563; P:negative regulation of vascular endothelial cell proliferation; IDA:BHF-UCL.
DR GO; GO:0001503; P:ossification; IMP:MGI.
DR GO; GO:0001649; P:osteoblast differentiation; IMP:MGI.
DR GO; GO:0045780; P:positive regulation of bone resorption; IMP:MGI.
DR GO; GO:0001819; P:positive regulation of cytokine production; IDA:MGI.
DR GO; GO:0045672; P:positive regulation of osteoclast differentiation; ISO:MGI.
DR GO; GO:0009791; P:post-embryonic development; IDA:MGI.
DR GO; GO:0046850; P:regulation of bone remodeling; ISO:MGI.
DR GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR Pfam; PF00008; EGF; 4.
DR SMART; SM00181; EGF; 6.
DR SMART; SM00179; EGF_CA; 4.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS00022; EGF_1; 5.
DR PROSITE; PS01186; EGF_2; 6.
DR PROSITE; PS50026; EGF_3; 6.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Disulfide bond; EGF-like domain;
KW Glycoprotein; Membrane; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..385
FT /note="Protein delta homolog 1"
FT /id="PRO_0000007520"
FT CHAIN 24..305
FT /note="Fetal antigen 1"
FT /id="PRO_0000007521"
FT TOPO_DOM 24..305
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 306..329
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 330..385
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 24..55
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 53..86
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 88..125
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 127..168
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 172..208
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 210..247
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT CARBOHYD 94
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:9118998"
FT /id="CAR_000160"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:9118998"
FT /id="CAR_000183"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine; atypical; partial"
FT /evidence="ECO:0000269|PubMed:9118998"
FT CARBOHYD 174
FT /note="N-linked (GlcNAc...) asparagine; atypical"
FT /evidence="ECO:0000269|PubMed:9118998"
FT CARBOHYD 216
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:9118998"
FT /id="CAR_000161"
FT CARBOHYD 224
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:9118998"
FT /id="CAR_000162"
FT CARBOHYD 258
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:9118998"
FT CARBOHYD 267
FT /note="O-linked (GalNAc...) threonine; partial"
FT /evidence="ECO:0000269|PubMed:9118998"
FT CARBOHYD 271
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:9118998"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 26..37
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 30..43
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 45..54
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 57..68
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 63..74
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 76..85
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 92..103
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 97..113
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 115..124
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 131..144
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 138..156
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 158..167
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 176..187
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 181..196
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 198..207
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 214..225
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 219..235
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 237..246
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT VAR_SEQ 211..305
FT /note="Missing (in isoform D2)"
FT /evidence="ECO:0000305"
FT /id="VSP_001379"
FT VAR_SEQ 211..303
FT /note="Missing (in isoform D)"
FT /evidence="ECO:0000305"
FT /id="VSP_001378"
FT VAR_SEQ 231..305
FT /note="Missing (in isoform C2)"
FT /evidence="ECO:0000305"
FT /id="VSP_001382"
FT VAR_SEQ 231..303
FT /note="Missing (in isoform C)"
FT /evidence="ECO:0000305"
FT /id="VSP_001381"
FT VAR_SEQ 231..281
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000305"
FT /id="VSP_001380"
FT VARIANT 347
FT /note="Missing"
FT /evidence="ECO:0000269|PubMed:7711066"
FT CONFLICT 250
FT /note="R -> P (in Ref. 2; AAA37175)"
FT /evidence="ECO:0000305"
FT CONFLICT 320..385
FT /note="VLGTVAIVFLNKCETWVSNLRYNHTFRKKKNLLLQYNSGEELAVNIIFPEKI
FT DMTTFNKEAGDEEI -> CWAPWPSSFSTSAKPGCPTCATTTCFARRRTSCCSITAARS
FT WRSISSSPRRLT (in Ref. 2; AAA37175)"
FT /evidence="ECO:0000305"
FT CONFLICT 344..345
FT /note="TF -> ML (in Ref. 4; BAA04121)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 385 AA; 41320 MW; E79864FEA5AF4FF1 CRC64;
MIATGALLRV LLLLLAFGHS TYGAECDPPC DPQYGFCEAD NVCRCHVGWE GPLCDKCVTA
PGCVNGVCKE PWQCICKDGW DGKFCEIDVR ACTSTPCANN GTCVDLEKGQ YECSCTPGFS
GKDCQHKAGP CVINGSPCQH GGACVDDEGQ ASHASCLCPP GFSGNFCEIV AATNSCTPNP
CENDGVCTDI GGDFRCRCPA GFVDKTCSRP VSNCASGPCQ NGGTCLQHTQ VSFECLCKPP
FMGPTCAKKR GASPVQVTHL PSGYGLTYRL TPGVHELPVQ QPEQHILKVS MKELNKSTPL
LTEGQAICFT ILGVLTSLVV LGTVAIVFLN KCETWVSNLR YNHTFRKKKN LLLQYNSGEE
LAVNIIFPEK IDMTTFNKEA GDEEI
