DLK2_PIG
ID DLK2_PIG Reviewed; 383 AA.
AC B2LW77; F1RRJ8;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 2.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Protein delta homolog 2;
DE Short=DLK-2;
DE AltName: Full=Epidermal growth factor-like protein 9;
DE Short=EGF-like protein 9;
DE Flags: Precursor;
GN Name=DLK2; Synonyms=EGFL9;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Wang J., Yang G.-Y., Li H.-J., Wang Y.-L., Zhao W.-D., Wang W.-J.,
RA Zhang Z.-Q.;
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Porcine genome sequencing project;
RL Submitted (OCT-2008) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; EU589332; ACB88022.1; -; mRNA.
DR EMBL; CU928765; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001121938.1; NM_001128466.1.
DR RefSeq; XP_005666087.1; XM_005666030.2.
DR RefSeq; XP_005666088.1; XM_005666031.2.
DR AlphaFoldDB; B2LW77; -.
DR SMR; B2LW77; -.
DR STRING; 9823.ENSSSCP00000001830; -.
DR PaxDb; B2LW77; -.
DR Ensembl; ENSSSCT00000001877; ENSSSCP00000001830; ENSSSCG00000001682.
DR GeneID; 100145892; -.
DR KEGG; ssc:100145892; -.
DR CTD; 65989; -.
DR VGNC; VGNC:87334; DLK2.
DR eggNOG; KOG1217; Eukaryota.
DR eggNOG; KOG1219; Eukaryota.
DR GeneTree; ENSGT00940000160761; -.
DR HOGENOM; CLU_039179_1_0_1; -.
DR InParanoid; B2LW77; -.
DR OrthoDB; 880666at2759; -.
DR TreeFam; TF351835; -.
DR Proteomes; UP000008227; Chromosome 7.
DR Proteomes; UP000314985; Unplaced.
DR Bgee; ENSSSCG00000001682; Expressed in frontal cortex and 19 other tissues.
DR ExpressionAtlas; B2LW77; baseline.
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; IEA:Ensembl.
DR GO; GO:0005112; F:Notch binding; IBA:GO_Central.
DR GO; GO:0045746; P:negative regulation of Notch signaling pathway; IEA:Ensembl.
DR GO; GO:0045598; P:regulation of fat cell differentiation; IEA:Ensembl.
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 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..383
FT /note="Protein delta homolog 2"
FT /id="PRO_0000410796"
FT TOPO_DOM 27..306
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 307..327
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 328..383
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 CONFLICT 18
FT /note="A -> G (in Ref. 1; ACB88022)"
FT /evidence="ECO:0000305"
FT CONFLICT 108
FT /note="I -> V (in Ref. 1; ACB88022)"
FT /evidence="ECO:0000305"
FT CONFLICT 250
FT /note="V -> A (in Ref. 1; ACB88022)"
FT /evidence="ECO:0000305"
FT CONFLICT 281
FT /note="S -> G (in Ref. 1; ACB88022)"
FT /evidence="ECO:0000305"
FT CONFLICT 304
FT /note="K -> E (in Ref. 1; ACB88022)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 383 AA; 40622 MW; C2D8E895BD815605 CRC64;
MPSGCRCLHL VCLLCILAAP VKPVRADDCS SHCDLAHGCC APDGSCRCDP GWEGLHCERC
VRMPGCQHGT CHQPWQCICH SGWAGKFCDK DEHVCTTQSP CRNGGQCIYD GGGEYHCVCP
PGFHGRDCER KEGPCEQAGS PCRNGGQCQD DQGFALNYTC RCLAGFVGAH CEVNVDDCLM
RPCANGATCL DGINRFSCLC PEGFAGRFCT INLDDCASRP CQRGARCRDR VHDFDCLCPS
GYGGKTCELV LPVPDPATTA DIPPGPTLAV VVPATGPIPH SAGAGLLRIS VKEVVRRQEA
GLGKSSLVAV VVFGAVTATL VLSTVLLTLR AWRRGVCPPG PCCYPAPHYA PARQDQECQV
SMLPAGLPLP PDLPPEPGKT TAL
