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Database: UniProt
Entry: DLK2_PIG
LinkDB: DLK2_PIG
Original site: 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   27-MAR-2024, entry version 87.
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}.
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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.ENSSSCP00000001831; -.
DR   GlyCosmos; B2LW77; 1 site, No reported glycans.
DR   PaxDb; 9823-ENSSSCP00000001830; -.
DR   Ensembl; ENSSSCT00000001877.4; ENSSSCP00000001830.1; ENSSSCG00000001682.5.
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; 5475408at2759; -.
DR   TreeFam; TF351835; -.
DR   Proteomes; UP000008227; Chromosome 7.
DR   Proteomes; UP000314985; Unplaced.
DR   Proteomes; UP000694570; Unplaced.
DR   Proteomes; UP000694571; Unplaced.
DR   Proteomes; UP000694720; Unplaced.
DR   Proteomes; UP000694722; Unplaced.
DR   Proteomes; UP000694723; Unplaced.
DR   Proteomes; UP000694724; Unplaced.
DR   Proteomes; UP000694725; Unplaced.
DR   Proteomes; UP000694726; Unplaced.
DR   Proteomes; UP000694727; Unplaced.
DR   Proteomes; UP000694728; Unplaced.
DR   Bgee; ENSSSCG00000001682; Expressed in frontal cortex and 19 other cell types or tissues.
DR   ExpressionAtlas; B2LW77; baseline.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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   CDD; cd00054; EGF_CA; 4.
DR   Gene3D; 2.10.25.10; Laminin; 5.
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   PANTHER; PTHR24049; CRUMBS FAMILY MEMBER; 1.
DR   PANTHER; PTHR24049:SF19; PROTEIN CRUMBS HOMOLOG 2; 1.
DR   Pfam; PF21700; DL-JAG_EGF-like; 1.
DR   Pfam; PF00008; EGF; 3.
DR   Pfam; PF12661; hEGF; 1.
DR   PRINTS; PR00010; EGFBLOOD.
DR   SMART; SM00181; EGF; 6.
DR   SMART; SM00179; EGF_CA; 4.
DR   SUPFAM; SSF57196; EGF/Laminin; 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
//
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