DLK2_BOVIN
ID DLK2_BOVIN Reviewed; 383 AA.
AC A4FV93;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 94.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Basal ganglia;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2006) 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; BC123884; AAI23885.1; -; mRNA.
DR RefSeq; NP_001076963.1; NM_001083494.1.
DR RefSeq; XP_005223540.1; XM_005223483.2.
DR RefSeq; XP_005223541.1; XM_005223484.3.
DR RefSeq; XP_005223542.1; XM_005223485.3.
DR AlphaFoldDB; A4FV93; -.
DR SMR; A4FV93; -.
DR STRING; 9913.ENSBTAP00000007690; -.
DR PaxDb; A4FV93; -.
DR Ensembl; ENSBTAT00000007690; ENSBTAP00000007690; ENSBTAG00000005850.
DR GeneID; 540262; -.
DR KEGG; bta:540262; -.
DR CTD; 65989; -.
DR VEuPathDB; HostDB:ENSBTAG00000005850; -.
DR VGNC; VGNC:28093; DLK2.
DR eggNOG; KOG1217; Eukaryota.
DR eggNOG; KOG1219; Eukaryota.
DR GeneTree; ENSGT00940000160761; -.
DR HOGENOM; CLU_039179_1_0_1; -.
DR InParanoid; A4FV93; -.
DR OMA; QECQVGM; -.
DR OrthoDB; 880666at2759; -.
DR TreeFam; TF351835; -.
DR Proteomes; UP000009136; Chromosome 23.
DR Bgee; ENSBTAG00000005850; Expressed in olfactory segment of nasal mucosa and 84 other tissues.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0045746; P:negative regulation of Notch signaling pathway; IEA:Ensembl.
DR GO; GO:0007219; P:Notch signaling pathway; IBA:GO_Central.
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_0000410795"
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 REGION 364..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 383 AA; 40507 MW; ED3014C48455F80D CRC64;
MPSGCRCLHL VCLLCILGAP VKPARGNDCS SLCDLAHGCC APDGSCRCDP GWEGLHCERC
VRMPGCQHGT CHQPWQCICH TGWAGKFCDK DEHICTTQSP CRNGGQCVYD GGGDYHCVCP
PGFHGRDCER KAGPCEQAGS PCRNGGQCQD DQGFALNFTC RCLAGFMGAR CEVNVDDCLM
RPCANGATCL DGINRFSCLC PEGFTGRFCT INLDDCASRP CQRGARCRDR VHDFDCLCPS
GYGGKTCELV LPVPGPAATA DSPPGPTLAV LVPATGPIPH SAGAGLLRIS VKEVVRRQEA
GLGEPSLVAV VVFGAVTAAL VLSTVLLTLR AWRRGFCPPG PCCYPAPHYA PARQDQECQV
SMLPTGLPLP PDLPPEPGKT TAL
