ID A0A3B4U7M0_SERDU Unreviewed; 1009 AA.
AC A0A3B4U7M0;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Protein crumbs homolog 1-like {ECO:0000313|Ensembl:ENSSDUP00000014606.1};
OS Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000014606.1, ECO:0000313|Proteomes:UP000261420};
RN [1] {ECO:0000313|Ensembl:ENSSDUP00000014606.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 AlphaFoldDB; A0A3B4U7M0; -.
DR Ensembl; ENSSDUT00000014886.1; ENSSDUP00000014606.1; ENSSDUG00000010516.1.
DR GeneTree; ENSGT00950000183101; -.
DR Proteomes; UP000261420; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0048513; P:animal organ development; IEA:UniProt.
DR CDD; cd00054; EGF_CA; 6.
DR CDD; cd00110; LamG; 3.
DR Gene3D; 2.60.120.200; -; 3.
DR Gene3D; 2.10.25.10; Laminin; 9.
DR InterPro; IPR013320; ConA-like_dom_sf.
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; IPR001791; Laminin_G.
DR PANTHER; PTHR24049; CRUMBS FAMILY MEMBER; 1.
DR PANTHER; PTHR24049:SF22; DROSOPHILA CRUMBS HOMOLOG; 1.
DR Pfam; PF00008; EGF; 7.
DR Pfam; PF12661; hEGF; 1.
DR Pfam; PF02210; Laminin_G_2; 3.
DR PRINTS; PR00010; EGFBLOOD.
DR SMART; SM00181; EGF; 9.
DR SMART; SM00179; EGF_CA; 8.
DR SMART; SM00282; LamG; 3.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 3.
DR SUPFAM; SSF57196; EGF/Laminin; 4.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 4.
DR PROSITE; PS00022; EGF_1; 8.
DR PROSITE; PS01186; EGF_2; 7.
DR PROSITE; PS50026; EGF_3; 9.
DR PROSITE; PS01187; EGF_CA; 2.
DR PROSITE; PS50025; LAM_G_DOMAIN; 3.
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}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|SAM:Phobius}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 946..969
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 22..64
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 66..107
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 111..292
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 294..330
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 336..505
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 507..543
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 569..742
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 744..780
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 782..817
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 819..855
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 859..896
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 898..934
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DISULFID 97..106
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 320..329
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 533..542
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 770..779
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 786..796
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 807..816
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 845..854
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 886..895
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 924..933
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1009 AA; 111146 MW; AEE246868BD69236 CRC64;
MLMQVDCCLT VSPLAGVHCE VDINECDSHP CQNGASCEDA ANAYRCHCPP PEPDQEPWGG
RDCDVRLVGC QQHQCQHEAG CVPMLTDDGE QSYACLCPPG WSGERCNTST TFSFNSEGYI
HMQLPVSKNR TRREADDHGL HMQLRFKSTL PDMVLYYRGT VEQFVSLELV SGSLQAWVKA
GKVLHVVYPG PVNDGEWHQV SVTMDERLVL SIKGPGCEEG CRVKNEGHNH LIFLQPSSFQ
QLYVGGAPQE YLAHTTSGRG FVGCMEDLYV DHKLLLPQDL IREENHGLEL GCTKTDWCQE
DPCLQRGQCV DMWVRASCQC QRPFYGESCE REYPSWTFGH ENTSSYSAYN ILESHGNNFS
ISFLMRSLKH NGLLLQLSRD GDPYLTIYLK EGTVAIYSPH TTLLSEATFV TDGNNNLVTV
KVHNGHVVFP KAGNHRALGN VSVEAGDVAY VGALPVGNSM NAWGGNFKGC LQDVRLDHKH
LTMEDYPETV EVYQASTEEN VLPGCHSDDT CKDEPCFNGG QCQVTWNDFK CDCSINYSGR
LCETRLWCVD NPCFDGVRCV DLQDGYECLT EAIFQDNSLQ YFANSSLLSP VTRITMDIRT
RDENGILLRA AGRAEVFCLG LLNSSLLVKL DSGVSSELLA FTSDRTVADG VWHHVQLTMV
DPAQSVSRWR LTVDGQRVGG SFGVGGNLNF LNDTKIWLAE KYTGCLGEVR VGGVYLPLIR
VPEAPQVSWF SRLGGHEPII GCQGAPICDS QPCLNQGECL DQFYEFNCSC SSGWEGELCE
TEINECSSGP CVYGTCKDLL ADYQCDCEPG YTGKDCQEEL DNCLEFSCVN GGSCVEMVGT
HTCLCPPGYV GKRCQWRFPP VACDAKTECL NGGICIGGNS GGNCTCKPGY TGARCETEID
ECESSPCLNG ATCLDRLNHF LCVCVPGFSG ALCESNKEEH KERVPWLAVT IPLTTLCVLL
AILVVFFLIM TARKKRQSEG TYSPSSQEVA GARLEMGSVL KVPPEERLI
//
