ID A0A1S3W6Y7_ERIEU Unreviewed; 1511 AA.
AC A0A1S3W6Y7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Deleted in malignant brain tumors 1 protein {ECO:0000256|ARBA:ARBA00014650};
DE AltName: Full=Hensin {ECO:0000256|ARBA:ARBA00030560};
GN Name=LOC103110527 {ECO:0000313|RefSeq:XP_016042141.1};
OS Erinaceus europaeus (Western European hedgehog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC Erinaceus.
OX NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_016042141.1};
RN [1] {ECO:0000313|RefSeq:XP_016042141.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the DMBT1 family.
CC {ECO:0000256|ARBA:ARBA00009931}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00059}.
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DR RefSeq; XP_016042141.1; XM_016186655.1.
DR CTD; 1755; -.
DR eggNOG; ENOG502QQ5W; Eukaryota.
DR InParanoid; A0A1S3W6Y7; -.
DR OrthoDB; 2950317at2759; -.
DR Proteomes; UP000079721; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR CDD; cd00041; CUB; 2.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 2.
DR Gene3D; 3.10.250.10; SRCR-like domain; 6.
DR Gene3D; 2.60.40.4100; Zona pellucida, ZP-C domain; 1.
DR Gene3D; 2.60.40.3210; Zona pellucida, ZP-N domain; 1.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR InterPro; IPR001190; SRCR.
DR InterPro; IPR017448; SRCR-like_dom.
DR InterPro; IPR036772; SRCR-like_dom_sf.
DR InterPro; IPR042235; ZP-C.
DR InterPro; IPR001507; ZP_dom.
DR PANTHER; PTHR48071; SRCR DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR48071:SF15; SRCR DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00431; CUB; 2.
DR Pfam; PF00530; SRCR; 6.
DR Pfam; PF00100; Zona_pellucida; 1.
DR PRINTS; PR00258; SPERACTRCPTR.
DR SMART; SM00042; CUB; 2.
DR SMART; SM00202; SR; 6.
DR SMART; SM00241; ZP; 1.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 2.
DR SUPFAM; SSF56487; SRCR-like; 6.
DR PROSITE; PS01180; CUB; 2.
DR PROSITE; PS00420; SRCR_1; 4.
DR PROSITE; PS50287; SRCR_2; 6.
DR PROSITE; PS51034; ZP_2; 1.
PE 3: Inferred from homology;
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW Differentiation {ECO:0000256|ARBA:ARBA00022782};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00196}; Membrane {ECO:0000256|SAM:Phobius};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW Reference proteome {ECO:0000313|Proteomes:UP000079721};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1511
FT /note="Deleted in malignant brain tumors 1 protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010262904"
FT TRANSMEM 1476..1495
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 34..134
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 189..289
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 324..424
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 538..638
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 688..788
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 815..926
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 932..1035
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 1058..1167
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 1176..1424
FT /note="ZP"
FT /evidence="ECO:0000259|PROSITE:PS51034"
FT REGION 146..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 433..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..449
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 59..123
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 72..133
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 103..113
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 214..278
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 227..288
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 258..268
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 349..413
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 362..423
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 393..403
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 563..627
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 576..637
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 607..617
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 713..777
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 726..787
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 757..767
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 960..1024
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 973..1034
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 1004..1014
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
SQ SEQUENCE 1511 AA; 164839 MW; 5B4A2DE18B1F38D1 CRC64;
MGISTGILQV CLFLSQVLAT ASQSELYTTP GLPVRLMDGG HPCEGRVEVL YGGFWSTVCD
DDWDEQDAEV VCRQLGCGPS VSALGGAEFG QGSGNILWGS VHCSGNESFL SHCRNSGWYN
HDCGHKEDAG AVCSEATFSF TMEDQRSETT LPTTMEETTE TTVPTTVEET TDWWHTENLS
YGTESGLALR LVNGGDRCQG RVEVLYRGTW GTVCDDSWDT NDANVVCRQL GCGWATSAPG
SAQFGQGSGP IVLDDVRCSG QESYLWSCPH SGWNSHNCNH GEDAGVVCSA SSSTPHPPPE
LYPSDHAMSA FSCLLVGTES GLALRLVNGG DRCRGRVEVL YRGTWGTVCD DSWDTKDANV
VCRQLGCGWA MSAPGSAQFG QGSGPIVLDD VNCSGHESYL WHCPHRGWNS HNCNHGEDAG
VICSVAQTSS PTTGWWPPPT ATTESKSHDI PPKAQYLTLP PRLVDHNPLL CCSTSCLRTQ
QACGHFPSSK GLQTQLETSV QIHSTAWPET LFPTALEETS ATYPLSTNWP GTESGLALRL
VNGGDRCRGR VEVLYRGTWG TVCDDSWDTK DANVVCRQLG CGWATSAPGS AQFGQGSGPI
VLDDVNCSGH ESYLWHCPHR GWNSHNCNHG EDAGVICSAS QSSSTTADNW TPSTFTTTRT
PTTAQTTYIP DWWRTTTPYY GTETGLALRL VNGGDRCRGR VEVLYRGTWG TVCDDSWDTK
DANVVCRQLG CGWATSAPGS AQFGQGSGPI VLDDVRCSGH ESYLWHCPHS GWNSHNCNHR
EDAGVVCSAV QTSSPTPDWW HTSTSITAGP PSPPCGGFLL NSSGTFSSPF YPGYYPNNAK
CVWNIEVRPG YRISLGFNDV QLETHSACSY DYVEIFDGPL NSSNLLGRIC NNTRQIYTSS
YNQMTVQFRS DVSFQNTGFV AWYNSFPRDV HLRLAGRNTS DSTCAGRVEI YHSGSWGTVC
DDSWSIQDAQ VVCRQLGCGD AVSAPSNAFF GPGSGPIALD DVQCSGSESY LWQCRNGGWF
SHNCGHQEDA GVICSGSLVS TPAPNYTTAI YPNTNLSCGG FLTQPSGSFS SPSYPSNYPN
NARCVWDIEV QNNDLVTVIF RDVQFESGCY HDYIEVYDGP YQSSPLLARV CDGSRGSFTS
SSNFMSVRFI SDGSVTRRGF RADYYSTPSN HNTKLLCLPK HMQASVSMSY LQSLGYSAWD
ISIASWNGSH QCQPQITPSQ VTFTIPYTGC GTTRQVDKDT ISYSNFLRAT VSSGIITRKN
SLNIHVLCRM LQDSWVDIMY ITNDTVELRE LQYGNFHVNV SFFTSPSFTH AVTGSPYYVD
LNQNLLVQAQ ILHADRSLSL FVDTCVASPS PHDFTSLTYD LIRNGCVKDE TYLPLPSPAP
HLARFQFRSF HFLHRFPSVY LHCKMVVCRP HDPSSRCYRG CVVRSKRDVS SGQQKVDVVL
GPLQLHAPRV QKRSLDLPMT DAEEQASTQQ NTHTTAVFVG VFVVAMVLAV AALALGRSSH
TACSHDLSTE M
//
