ID A0A452ISV3_9SAUR Unreviewed; 1191 AA.
AC A0A452ISV3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Delta-like protein {ECO:0000256|RuleBase:RU280815};
OS Gopherus agassizii (Agassiz's desert tortoise).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Testudinidae; Gopherus.
OX NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000031207.1, ECO:0000313|Proteomes:UP000291020};
RN [1] {ECO:0000313|Proteomes:UP000291020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28562605;
RA Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT "The Agassiz's desert tortoise genome provides a resource for the
RT conservation of a threatened species.";
RL PLoS ONE 12:e0177708-e0177708(2017).
RN [2] {ECO:0000313|Ensembl:ENSGAGP00000031207.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 AlphaFoldDB; A0A452ISV3; -.
DR STRING; 38772.ENSGAGP00000031207; -.
DR Ensembl; ENSGAGT00000035394.1; ENSGAGP00000031207.1; ENSGAGG00000022427.1.
DR Proteomes; UP000291020; 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:0005112; F:Notch binding; IEA:InterPro.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:InterPro.
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; PTHR24033; EGF-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24033:SF151; PROTEIN EYES SHUT; 1.
DR Pfam; PF21700; DL-JAG_EGF-like; 1.
DR Pfam; PF01414; DSL; 1.
DR Pfam; PF00008; EGF; 10.
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; SM00214; VWC; 1.
DR SMART; SM00215; VWC_out; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 6.
DR SUPFAM; SSF57603; FnI-like domain; 1.
DR SUPFAM; SSF57184; Growth factor receptor domain; 2.
DR PROSITE; PS00010; ASX_HYDROXYL; 10.
DR PROSITE; PS51051; DSL; 1.
DR PROSITE; PS00022; EGF_1; 15.
DR PROSITE; PS01186; EGF_2; 11.
DR PROSITE; PS50026; EGF_3; 15.
DR PROSITE; PS01187; EGF_CA; 3.
PE 4: Predicted;
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 Reference proteome {ECO:0000313|Proteomes:UP000291020};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|RuleBase:RU280815};
KW Signal {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 TRANSMEM 1041..1066
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 158..202
FT /note="DSL"
FT /evidence="ECO:0000259|PROSITE:PS51051"
FT DOMAIN 203..236
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 269..307
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 309..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..458
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 460..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 563..600
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 602..638
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 640..676
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 678..714
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 717..753
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 755..791
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 793..829
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 1124..1191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1124..1142
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1162..1182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 160..169
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00377"
FT DISULFID 173..185
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00377"
FT DISULFID 193..202
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00377"
FT DISULFID 226..235
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 297..306
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
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 427..437
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 448..457
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 590..599
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 628..637
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 666..675
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 704..713
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 743..752
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 781..790
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 819..828
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1191 AA; 130982 MW; DBB55B7D75001D7D CRC64;
MTRASGQFEL EILSMQNVNG ELQNGNCCDG PRNPGDRKCT KDECDTYFKV CLKEYQSRVS
AGGPCSFGSG STPVIGGNTF NLKYNRNNER NRIVLPFSFA WPRSYTLLVE AWDYSNDTAN
PDSIIEKASH SGMINPSRQW QTLKQNAGIA HFEYQIRVTC DEHYYGFGCN KFCRPRDDFF
GHHTCDQNGN KTCLEGWMGP ECSKAICRQG CSPKHGSCKI PGECRCQYGW QGQYCDKCIP
HPGCVHGTCI EPWQCLCETN WGGQLCDKDL NYCGTHPPCL NGGTCSNTGP DKYQCACPEG
YSGQNCEIAE HACLSDPCHN GGSCLETSTG FECVCTPGWA GPTCTLNIDD CSPNPCGHGG
TCQDLIDGFK CICPPQWTGK TCQLDANECE GKPCVNANSC RNLIGSYYCD CIAGWSGQNC
DININDCLGQ CQNGGSCRDL VNGYRCICPP GYAGDHCEKD INECASNPCL NGGHCQDEIN
GFQCLCPAGF SGNLCQLDID YCEPNPCQNG AQCFNLNTDY FCNCSEDYEG KNCSHLKDHC
RTTPCEVIDS CTVAVASNST PEGVRYISSN VCGPHGKCKS QAGGKFTCEC NKGFTGTYCH
ENINDCESNP CKNGGTCIDG INSYKCICSD GWEGVYCETN INDCSKNPCH NGGTCRDLVN
DFFCECKNGW KGKTCHSRDS QCDEATCNNG GTCYDEGDTF KCMCPAGWEG ATCNIARNSS
CLPNPCHNGG TCVISADSFT CVCKEGWEGP TCTQNTNDCS PHPCYNSGTC VDGDNWYRCE
CAPGFAGPDC RININECQSS PCAFGATCVD EINGYRCICP PGRSGPRCQE VTGRPCINNG
RVMSDGAKWD DDCNTCQCWN GKVACSKVWC GPRPCLIHAK GHECPAGHTC VPIKDDHCFT
HPCSGVGVCW PSNQQPVKTK CNSDSYYQDN CANITFTFNK ELMVSGLTTE HICSDLRNLN
ILKNVSVEYS IYITCEPSHL ANNEIHVAIS AEDIGKDENP VKEITDKIID LVSKRDGNNT
LIAAVAEVRV QRRPIKNKTD FLVPLLSSVL TVAWICCLVT AFFWCVRKRR KQSSHTHTAS
DDNTTNNVRE QLNQIKNPIE KHGANTVPIK DYENKNSKIA KIRTHNSEVE EDDMDKHQQK
SRFVKQPAYT LVDRDEKPPN STPTKHPNWT NKQDNRDLES AQSLNRMEYI V
//
