ID G1SLN5_RABIT Unreviewed; 360 AA.
AC G1SLN5;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 2.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=Delta like non-canonical Notch ligand 2 {ECO:0000313|Ensembl:ENSOCUP00000003778.3};
GN Name=DLK2 {ECO:0000313|Ensembl:ENSOCUP00000003778.3};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000003778.3, ECO:0000313|Proteomes:UP000001811};
RN [1] {ECO:0000313|Ensembl:ENSOCUP00000003778.3, ECO:0000313|Proteomes:UP000001811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke inbred {ECO:0000313|Ensembl:ENSOCUP00000003778.3,
RC ECO:0000313|Proteomes:UP000001811};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSOCUP00000003778.3}
RP IDENTIFICATION.
RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000003778.3};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; AAGW02018017; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02018018; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02018019; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G1SLN5; -.
DR SMR; G1SLN5; -.
DR STRING; 9986.ENSOCUP00000003778; -.
DR PaxDb; 9986-ENSOCUP00000003778; -.
DR Ensembl; ENSOCUT00000004374.3; ENSOCUP00000003778.3; ENSOCUG00000004371.3.
DR eggNOG; KOG1217; Eukaryota.
DR GeneTree; ENSGT00940000160761; -.
DR HOGENOM; CLU_039179_1_0_1; -.
DR InParanoid; G1SLN5; -.
DR TreeFam; TF351835; -.
DR Proteomes; UP000001811; Chromosome 12.
DR Bgee; ENSOCUG00000004371; Expressed in brain and 8 other cell types or tissues.
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: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; 3.
DR Gene3D; 2.10.25.10; Laminin; 5.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR PANTHER; PTHR24044; NOTCH LIGAND FAMILY MEMBER; 1.
DR PANTHER; PTHR24044:SF423; PROTEIN DELTA HOMOLOG 2; 1.
DR Pfam; PF21700; DL-JAG_EGF-like; 1.
DR Pfam; PF00008; EGF; 3.
DR PRINTS; PR00010; EGFBLOOD.
DR SMART; SM00181; EGF; 5.
DR SMART; SM00179; EGF_CA; 3.
DR SUPFAM; SSF57196; EGF/Laminin; 3.
DR PROSITE; PS00010; ASX_HYDROXYL; 2.
DR PROSITE; PS00022; EGF_1; 5.
DR PROSITE; PS01186; EGF_2; 4.
DR PROSITE; PS50026; EGF_3; 4.
DR PROSITE; PS01187; EGF_CA; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000001811};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..360
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5023841038"
FT TRANSMEM 284..306
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 25..58
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 109..149
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 151..187
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 189..225
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DISULFID 48..57
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 139..148
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 177..186
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 215..224
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 360 AA; 37884 MW; A6FD46D5676604C1 CRC64;
MPSGCRCLRL VCLLCILGAP GQPARADDCS SHCDLAHGCC APDGSCRCDP GWEGLHCERC
VRMPGCQHGT CHQPWQCICH SGWAGKFCDK AGLCPAPPRS CQELSIHVLS RPSLPSSPCR
NGGQCQDDRG FALNFTCRCL AGFVGARCEL NVDDCLMRPC ANGATCLDGI NRFSCLCPEG
FAGRFCTINL DDCASHPCQR GARCRDRVHD FDCLCPSGYG GKTCELVLPV AEPPTTAGTP
LGPSSAAVAP VTGPAPHSAG AGLLRISVKE VVRRQDAGLG ESSLVVLVVF GALTAALVLA
TMLLTLRAWR RGVCPPGPCC HPAPHYAPPC QDQECQVSML PTVLPPAPEL PPEPGKTTAL
//
