ID G3VAT1_SARHA Unreviewed; 1245 AA.
AC G3VAT1;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE RecName: Full=Delta-like protein {ECO:0000256|RuleBase:RU280815};
GN Name=JAG2 {ECO:0000313|Ensembl:ENSSHAP00000000285.1};
OS Sarcophilus harrisii (Tasmanian devil) (Sarcophilus laniarius).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Dasyuromorphia; Dasyuridae; Sarcophilus.
OX NCBI_TaxID=9305 {ECO:0000313|Ensembl:ENSSHAP00000000285.1, ECO:0000313|Proteomes:UP000007648};
RN [1] {ECO:0000313|Ensembl:ENSSHAP00000000285.1, ECO:0000313|Proteomes:UP000007648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21709235; DOI=10.1073/pnas.1102838108;
RA Miller W., Hayes V.M., Ratan A., Petersen D.C., Wittekindt N.E., Miller J.,
RA Walenz B., Knight J., Qi J., Zhao F., Wang Q., Bedoya-Reina O.C.,
RA Katiyar N., Tomsho L.P., Kasson L.M., Hardie R.A., Woodbridge P.,
RA Tindall E.A., Bertelsen M.F., Dixon D., Pyecroft S., Helgen K.M.,
RA Lesk A.M., Pringle T.H., Patterson N., Zhang Y., Kreiss A., Woods G.M.,
RA Jones M.E., Schuster S.C.;
RT "Genetic diversity and population structure of the endangered marsupial
RT Sarcophilus harrisii (Tasmanian devil).";
RL Proc. Natl. Acad. Sci. U.S.A. 108:12348-12353(2011).
RN [2] {ECO:0000313|Ensembl:ENSSHAP00000000285.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Putative Notch ligand involved in the mediation of Notch
CC signaling. {ECO:0000256|RuleBase:RU280815}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479,
CC ECO:0000256|RuleBase:RU280815}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU280815}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR RefSeq; XP_003756492.2; XM_003756444.2.
DR AlphaFoldDB; G3VAT1; -.
DR STRING; 9305.ENSSHAP00000000285; -.
DR Ensembl; ENSSHAT00000000290.2; ENSSHAP00000000285.1; ENSSHAG00000000250.2.
DR GeneID; 100921475; -.
DR KEGG; shr:100921475; -.
DR CTD; 3714; -.
DR eggNOG; KOG1217; Eukaryota.
DR GeneTree; ENSGT00940000160944; -.
DR HOGENOM; CLU_004732_0_0_1; -.
DR InParanoid; G3VAT1; -.
DR OMA; KGTNCHI; -.
DR OrthoDB; 5475408at2759; -.
DR TreeFam; TF351835; -.
DR Proteomes; UP000007648; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0008083; F:growth factor activity; IEA:Ensembl.
DR GO; GO:0005112; F:Notch binding; IEA:Ensembl.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:InterPro.
DR GO; GO:0042127; P:regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR GO; GO:0045061; P:thymic T cell selection; IEA:Ensembl.
DR CDD; cd00054; EGF_CA; 13.
DR Gene3D; 2.10.25.140; -; 1.
DR Gene3D; 2.60.40.3510; -; 1.
DR Gene3D; 2.10.25.10; Laminin; 15.
DR InterPro; IPR001774; DSL.
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 InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR026219; Jagged/Serrate.
DR InterPro; IPR011651; Notch_ligand_N.
DR InterPro; IPR001007; VWF_dom.
DR PANTHER; PTHR24044; NOTCH LIGAND FAMILY MEMBER; 1.
DR PANTHER; PTHR24044:SF421; PROTEIN JAGGED-2; 1.
DR Pfam; PF21700; DL-JAG_EGF-like; 1.
DR Pfam; PF01414; DSL; 1.
DR Pfam; PF00008; EGF; 10.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF12661; hEGF; 2.
DR Pfam; PF07657; MNNL; 1.
DR PRINTS; PR00010; EGFBLOOD.
DR PRINTS; PR02059; JAGGEDFAMILY.
DR SMART; SM00051; DSL; 1.
DR SMART; SM00181; EGF; 16.
DR SMART; SM00179; EGF_CA; 14.
DR SMART; SM00215; VWC_out; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 5.
DR SUPFAM; SSF57603; FnI-like domain; 1.
DR SUPFAM; SSF57184; Growth factor receptor domain; 2.
DR PROSITE; PS00010; ASX_HYDROXYL; 9.
DR PROSITE; PS51051; DSL; 1.
DR PROSITE; PS00022; EGF_1; 15.
DR PROSITE; PS01186; EGF_2; 10.
DR PROSITE; PS50026; EGF_3; 14.
DR PROSITE; PS01187; EGF_CA; 3.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473,
KW ECO:0000256|RuleBase:RU280815};
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}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|RuleBase:RU280815, ECO:0000256|SAM:Phobius};
KW Notch signaling pathway {ECO:0000256|ARBA:ARBA00022976};
KW Reference proteome {ECO:0000313|Proteomes:UP000007648};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|RuleBase:RU280815};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU280815};
KW Transmembrane {ECO:0000256|RuleBase:RU280815, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|RuleBase:RU280815,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1245
FT /note="Delta-like protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003457286"
FT TRANSMEM 1084..1107
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 196..240
FT /note="DSL"
FT /evidence="ECO:0000259|PROSITE:PS51051"
FT DOMAIN 307..345
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 347..383
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 385..421
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 423..459
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 461..496
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 498..534
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 536..572
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 596..634
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 636..672
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 674..710
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 712..748
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 751..787
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 789..825
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 827..863
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 1200..1245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1163..1193
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1225..1245
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 198..207
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00377"
FT DISULFID 211..223
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00377"
FT DISULFID 231..240
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00377"
FT DISULFID 335..344
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 373..382
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 411..420
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 449..458
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 465..475
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 486..495
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 524..533
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 562..571
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 624..633
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 662..671
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 700..709
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 738..747
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 777..786
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 815..824
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 853..862
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1245 AA; 137468 MW; 7FD315D6A56DFF77 CRC64;
MLEQSRRMAA TRLGLLFLTI WVQAAQSMGY FELQLSSVKN VNGELQNGNC CDSNRTAWPT
GSGWTCGRDE CDTYVRVCLK EYQTKVTPTG PCSYGHGATP VLGGNTFSLN GGSNTGRSGH
QDRGSRDRGR VIIPFQYAWP RSFTLIVEAW DWDNGTQNDG LLIERVSHAG MINPEDRWKS
LHFSGHVAHL EVKIRVQCDE NYYSSTCNKF CRPRDDFVGH YTCDQYGNKA CMEGWMGPEC
KQAVCKQGCN LLHGGCTVPG ECRCHYGWQG RFCDECVTYP GCLHGSCTEP WKCNCETNWG
GLLCDKDLNY CGSHHPCTNG GTCMNTEPDQ YQCACPDGYS GKNCEIVEHA CVSNPCANGG
SCHEVFSSFE CHCPSGWSGP TCAIDIDECA SNPCARGGTC IDQVNGFECI CPQQWVGTTC
QLDANECEGK PCLNAFSCKN LIGGYYCDCI PGWKGVNCHI NINDCQGQCQ NGGTCKDEVN
GYQCLCPRGF IGKHCELEKN ECASNPCQNR GLCEDLVDGF RCHCTKGFSG VFCEVDIDFC
EPYPCQNGAR CYSLEGDYYC ACPEDYDGKN CSYPKDHCRN GSCKVINSCE IEVFTNTTRF
ISSKVCGPHG HCISQPGGNF TCTCESGFTG TYCHENINDC LGMPCQNGGT CIDEVDSFQC
FCPSGWEGEL CDTNLNDCFP DPCHNGGHCI DLLNDFYCEC RDGWKGKTCH SREYQCDANT
CSNGGTCYDS GDTFRCICPP EWKGSTCNTA RNSSCLLNPC MNGGTCVGSG DSFSCICKDG
WEGRTCTQNT NDCNPHPCYN GGICVDGVNW FRCNCAPGFA GPDCRINIDE CQSSPCAYGA
TCVDEINGYQ CICPPGRAGQ RCQEVIRFGK SCWSQGMPFP HGSKWTEECN TCHCMDGRIE
CSTVWCGRKP CLLPKHPDYT ENQCPRGQDC LERAYPKCLQ PPCAAWGECS PVEPLVPSTP
CQPNSGHLGN NCAKITLIFN RDKIPQGTTV GAICAGIRYL PATRAAAQEG LLVLLCDLSA
STENAVEVAI SFSPPRDEPD NILIQNAANT IVSAITKPEN STVLLAVTEV KVETVVMGNS
STDYLVPILC GVFSIMWLTC IIICVWWTRK RRKERERSRL PREESVNNQW ATLNPIRNPI
DKPYSNKDIY YECKNFISPP KRTHDEVEEY VEYEEEEDEE EEEEGEREVI EVEKFLSPKL
QKSSLTKGPG DFKESPLGKW AHPGASHKVD NRSLKNVNDY EDGKD
//