GenomeNet

Database: UniProt
Entry: Q09163
LinkDB: Q09163
Original site: Q09163 
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   10-APR-2019, entry version 162.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   STRAIN=SWR/J; TISSUE=Fibroblast;
RX   PubMed=8095043;
RA   Laborda J., Sausville E.A., Hoffman T., Notario V.;
RT   "dlk, a putative mammalian homeotic gene differentially expressed in
RT   small 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;
RA   Lee Y.L., Helman L., Hoffman T., Laborda J.;
RT   "dlk, pG2 and Pref-1 mRNAs encode similar proteins belonging to the
RT   EGF-like superfamily. Identification of polymorphic variants of this
RT   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
RT   encoding 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
RT   fetal antigen 1 (mFA1) -- the circulating gene product of the delta-
RT   like protein (dlk), preadipocyte factor 1 (Pref-1) and stromal-cell-
RT   derived protein 1 (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.,
RA   Diaz-Guerra M.J., 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.
CC       Inhibits 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
CC       protein. 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,
CC       adult adrenal gland, brain, testis and ovary and, to a lesser
CC       degree, in adult kidney, muscle, thymus and heart.
CC       {ECO:0000269|PubMed:17320102}.
CC   -!- DEVELOPMENTAL STAGE: Expression is elevated in liver after birth
CC       but starts to decline around postnatal day 16.
CC       {ECO:0000269|PubMed:17320102}.
CC   -!- PTM: N- and O-glycosylated. {ECO:0000269|PubMed:9118998}.
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   UniGene; Mm.157069; -.
DR   ProteinModelPortal; Q09163; -.
DR   SMR; Q09163; -.
DR   BioGrid; 199231; 1.
DR   DIP; DIP-6010N; -.
DR   IntAct; Q09163; 1.
DR   STRING; 10090.ENSMUSP00000105470; -.
DR   GlyConnect; 153; -.
DR   iPTMnet; Q09163; -.
DR   PhosphoSitePlus; Q09163; -.
DR   UniCarbKB; Q09163; -.
DR   PaxDb; Q09163; -.
DR   PRIDE; Q09163; -.
DR   GeneID; 13386; -.
DR   KEGG; mmu:13386; -.
DR   CTD; 8788; -.
DR   MGI; MGI:94900; Dlk1.
DR   eggNOG; KOG1217; Eukaryota.
DR   eggNOG; ENOG410XP6K; LUCA.
DR   HOGENOM; HOG000072581; -.
DR   HOVERGEN; HBG007065; -.
DR   InParanoid; Q09163; -.
DR   OrthoDB; 619882at2759; -.
DR   PhylomeDB; Q09163; -.
DR   ChiTaRS; Dlk1; mouse.
DR   PRO; PR:Q09163; -.
DR   Proteomes; UP000000589; Unplaced.
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: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:0046851; P:negative regulation of bone remodeling; ISO: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: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; IPR013032; EGF-like_CS.
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; Complete proteome; Cytoplasm; Disulfide bond;
KW   EGF-like domain; Glycoprotein; Membrane; Reference proteome; Repeat;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     23       {ECO:0000255}.
FT   CHAIN        24    385       Protein delta homolog 1.
FT                                /FTId=PRO_0000007520.
FT   CHAIN        24    305       Fetal antigen 1.
FT                                /FTId=PRO_0000007521.
FT   TOPO_DOM     24    305       Extracellular. {ECO:0000255}.
FT   TRANSMEM    306    329       Helical. {ECO:0000255}.
FT   TOPO_DOM    330    385       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       24     55       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN       53     86       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN       88    125       EGF-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      127    168       EGF-like 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      172    208       EGF-like 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      210    247       EGF-like 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   CARBOHYD     94     94       O-linked (GalNAc...) serine.
FT                                {ECO:0000269|PubMed:9118998}.
FT                                /FTId=CAR_000160.
FT   CARBOHYD    100    100       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:9118998}.
FT                                /FTId=CAR_000183.
FT   CARBOHYD    165    165       N-linked (GlcNAc...) asparagine;
FT                                atypical; partial.
FT                                {ECO:0000269|PubMed:9118998}.
FT   CARBOHYD    174    174       N-linked (GlcNAc...) asparagine;
FT                                atypical. {ECO:0000269|PubMed:9118998}.
FT   CARBOHYD    216    216       O-linked (GalNAc...) serine.
FT                                {ECO:0000269|PubMed:9118998}.
FT                                /FTId=CAR_000161.
FT   CARBOHYD    224    224       O-linked (GalNAc...) threonine.
FT                                {ECO:0000269|PubMed:9118998}.
FT                                /FTId=CAR_000162.
FT   CARBOHYD    258    258       O-linked (GalNAc...) threonine.
FT                                {ECO:0000269|PubMed:9118998}.
FT   CARBOHYD    267    267       O-linked (GalNAc...) threonine; partial.
FT                                {ECO:0000269|PubMed:9118998}.
FT   CARBOHYD    271    271       O-linked (GalNAc...) threonine.
FT                                {ECO:0000269|PubMed:9118998}.
FT   CARBOHYD    295    295       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     26     37       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     30     43       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     45     54       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     57     68       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     63     74       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     76     85       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     92    103       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     97    113       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    115    124       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    131    144       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    138    156       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    158    167       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    176    187       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    181    196       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    198    207       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    214    225       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    219    235       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    237    246       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   VAR_SEQ     211    305       Missing (in isoform D2). {ECO:0000305}.
FT                                /FTId=VSP_001379.
FT   VAR_SEQ     211    303       Missing (in isoform D). {ECO:0000305}.
FT                                /FTId=VSP_001378.
FT   VAR_SEQ     231    305       Missing (in isoform C2). {ECO:0000305}.
FT                                /FTId=VSP_001382.
FT   VAR_SEQ     231    303       Missing (in isoform C). {ECO:0000305}.
FT                                /FTId=VSP_001381.
FT   VAR_SEQ     231    281       Missing (in isoform B). {ECO:0000305}.
FT                                /FTId=VSP_001380.
FT   VARIANT     347    347       Missing. {ECO:0000269|PubMed:7711066}.
FT   CONFLICT    250    250       R -> P (in Ref. 2; AAA37175).
FT                                {ECO:0000305}.
FT   CONFLICT    320    385       VLGTVAIVFLNKCETWVSNLRYNHTFRKKKNLLLQYNSGEE
FT                                LAVNIIFPEKIDMTTFNKEAGDEEI -> CWAPWPSSFSTS
FT                                AKPGCPTCATTTCFARRRTSCCSITAARSWRSISSSPRRLT
FT                                (in Ref. 2; AAA37175). {ECO:0000305}.
FT   CONFLICT    344    345       TF -> ML (in Ref. 4; BAA04121).
FT                                {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
//
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