DLK2_RAT
ID DLK2_RAT Reviewed; 382 AA.
AC D3ZUK3;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 68.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Regulates adipogenesis. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
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DR EMBL; CH473987; EDM18816.1; -; Genomic_DNA.
DR RefSeq; NP_001101672.1; NM_001108202.1.
DR RefSeq; XP_006244585.1; XM_006244523.3.
DR AlphaFoldDB; D3ZUK3; -.
DR SMR; D3ZUK3; -.
DR STRING; 10116.ENSRNOP00000025638; -.
DR GlyGen; D3ZUK3; 1 site.
DR PaxDb; D3ZUK3; -.
DR PRIDE; D3ZUK3; -.
DR Ensembl; ENSRNOT00000025638; ENSRNOP00000025638; ENSRNOG00000018949.
DR GeneID; 316232; -.
DR KEGG; rno:316232; -.
DR UCSC; RGD:1309143; rat.
DR CTD; 65989; -.
DR RGD; 1309143; Dlk2.
DR eggNOG; KOG1217; Eukaryota.
DR GeneTree; ENSGT00940000160761; -.
DR HOGENOM; CLU_039179_1_0_1; -.
DR InParanoid; D3ZUK3; -.
DR OMA; QECQVGM; -.
DR OrthoDB; 880666at2759; -.
DR PhylomeDB; D3ZUK3; -.
DR PRO; PR:D3ZUK3; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Proteomes; UP000234681; Chromosome 9.
DR Bgee; ENSRNOG00000018949; Expressed in frontal cortex and 3 other tissues.
DR Genevisible; D3ZUK3; RN.
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; ISO:RGD.
DR GO; GO:0005112; F:Notch binding; IBA:GO_Central.
DR GO; GO:0045746; P:negative regulation of Notch signaling pathway; ISO:RGD.
DR GO; GO:0045598; P:regulation of fat cell differentiation; ISO:RGD.
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 3: Inferred from homology;
KW Calcium; Disulfide bond; EGF-like domain; Glycoprotein; Membrane;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..382
FT /note="Protein delta homolog 2"
FT /id="PRO_0000410797"
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"
SQ SEQUENCE 382 AA; 40245 MW; 32C1A657F7CAEA54 CRC64;
MPSGCRCLNL VCLLCILGAT SQPARADDCS SHCDLAHGCC APDGSCRCDP GWEGLHCERC
VRMPGCQHGT CHQPWQCICH SGWAGKFCDK DEHICTSQSP CQNGGQCVYD GGGEYHCVCL
PGFRGRGCER KAGPCEQAGF PCQNGGQCQD NQGFALNFTC RCLAGFMGAH CEVNVDDCLM
RPCANGATCI DGINRFSCLC PEGFAGRFCT INLDDCASRP CQRGARCRDR VHDFDCLCPS
GYGGKTCELV LPAPDPATIG TPQAPASAVV VPATGSAPHS AGAGLLRISV KEVVRRQEAG
LGESSLVALV VFGSLTAALV LATVLLTLRA WRRGICPTGP CCDPAPHYAP ARQDQECQVS
MLPAGFPLSP DLPPEPGKTT AL
