GenomeNet

Database: UniProt
Entry: A4FV93
LinkDB: A4FV93
Original site: A4FV93 
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   16-JAN-2019, entry version 83.
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;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; 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}.
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   UniGene; Bt.24383; -.
DR   ProteinModelPortal; A4FV93; -.
DR   SMR; A4FV93; -.
DR   STRING; 9913.ENSBTAP00000007690; -.
DR   PaxDb; A4FV93; -.
DR   PRIDE; A4FV93; -.
DR   Ensembl; ENSBTAT00000007690; ENSBTAP00000007690; ENSBTAG00000005850.
DR   GeneID; 540262; -.
DR   KEGG; bta:540262; -.
DR   CTD; 65989; -.
DR   VGNC; VGNC:28093; DLK2.
DR   eggNOG; KOG1217; Eukaryota.
DR   eggNOG; KOG1219; Eukaryota.
DR   eggNOG; ENOG410ZHP6; LUCA.
DR   GeneTree; ENSGT00940000160761; -.
DR   HOGENOM; HOG000065685; -.
DR   HOVERGEN; HBG051454; -.
DR   InParanoid; A4FV93; -.
DR   OMA; FHGKDCE; -.
DR   OrthoDB; 880666at2759; -.
DR   TreeFam; TF351835; -.
DR   Proteomes; UP000009136; Chromosome 23.
DR   Bgee; ENSBTAG00000005850; Expressed in 6 organ(s), highest expression level in brain.
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:0042803; F:protein homodimerization activity; IEA:Ensembl.
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; Complete proteome; Disulfide bond; EGF-like domain;
KW   Glycoprotein; Membrane; Reference proteome; Repeat; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL        1     26       {ECO:0000255}.
FT   CHAIN        27    383       Protein delta homolog 2.
FT                                /FTId=PRO_0000410795.
FT   TOPO_DOM     27    306       Extracellular. {ECO:0000255}.
FT   TRANSMEM    307    327       Helical. {ECO:0000255}.
FT   TOPO_DOM    328    383       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       27     58       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN       62     89       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN       91    129       EGF-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      131    172       EGF-like 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      174    210       EGF-like 5; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      212    248       EGF-like 6; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   CARBOHYD    157    157       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     29     40       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     33     46       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     48     57       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     66     71       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     79     88       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     95    107       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    101    117       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    119    128       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    135    148       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    142    160       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    162    171       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    178    189       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    183    198       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    200    209       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    216    227       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    221    236       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    238    247       {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
//
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