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Database: UniProt
Entry: A0A3Q1ATD8_AMPOC
LinkDB: A0A3Q1ATD8_AMPOC
Original site: A0A3Q1ATD8_AMPOC 
ID   A0A3Q1ATD8_AMPOC        Unreviewed;      1321 AA.
AC   A0A3Q1ATD8;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Crumbs cell polarity complex component 1 {ECO:0000313|Ensembl:ENSAOCP00000004762.1};
OS   Amphiprion ocellaris (Clown anemonefish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Amphiprion.
OX   NCBI_TaxID=80972 {ECO:0000313|Ensembl:ENSAOCP00000004762.1, ECO:0000313|Proteomes:UP000257160};
RN   [1] {ECO:0000313|Ensembl:ENSAOCP00000004762.1}
RP   IDENTIFICATION.
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   Ensembl; ENSAOCT00000007540.1; ENSAOCP00000004762.1; ENSAOCG00000008332.1.
DR   GeneTree; ENSGT00940000155152; -.
DR   Proteomes; UP000257160; 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; 13.
DR   CDD; cd00110; LamG; 3.
DR   Gene3D; 2.60.120.200; -; 3.
DR   Gene3D; 2.10.25.10; Laminin; 15.
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:SF31; DELTA_NOTCH LIKE EGF REPEAT CONTAINING; 1.
DR   Pfam; PF00008; EGF; 9.
DR   Pfam; PF12661; hEGF; 1.
DR   Pfam; PF02210; Laminin_G_2; 3.
DR   PRINTS; PR00010; EGFBLOOD.
DR   SMART; SM00181; EGF; 15.
DR   SMART; SM00179; EGF_CA; 13.
DR   SMART; SM00282; LamG; 3.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 3.
DR   SUPFAM; SSF57196; EGF/Laminin; 10.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 7.
DR   PROSITE; PS00022; EGF_1; 13.
DR   PROSITE; PS01186; EGF_2; 9.
DR   PROSITE; PS50026; EGF_3; 15.
DR   PROSITE; PS01187; EGF_CA; 3.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000257160};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        1259..1285
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          45..81
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          83..119
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          121..157
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          159..196
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          198..234
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          236..292
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          294..336
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          338..378
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          380..568
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          570..606
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          612..784
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          786..822
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          849..1038
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          1040..1076
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1078..1113
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1115..1151
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1171..1209
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1211..1247
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   REGION          1293..1321
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        71..80
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        109..118
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        147..156
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        224..233
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        282..291
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        368..377
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        596..605
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        812..821
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        1066..1075
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        1082..1092
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        1103..1112
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        1141..1150
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        1199..1208
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        1237..1246
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   1321 AA;  144305 MW;  0A3D204F37B7637D CRC64;
     NITICSTSMI SNWISFCLES MMPSDVNISK HDLFIGASPD KLPPTVDQCS PNPCQNRAIC
     RLRGDGYSCF CVPGFQGARC QIDVNECASE PCSNGATCVD RVGRFSCLCS PGFTGVTCEV
     QIDECQSQPC LNGGSCHDYA GGYSCTCLSG FQGHRCEINI DECQEQPCQN GGLCIDGVNE
     YSCDCSHSAF TGRHCETPLP PCLSEPCFNS AICKDDHGNY TCECWPGFEG RHCEVDISEC
     SSSPCLRGGR CIERSWQALY GSEPLLPEHY DQRQAAGYIC SCPPGTTGSL CQEVINHCES
     SPCQNGGRCE SYVGGYICHC LKQSTDGILY GGVNCDVKLV GCEGHECQNQ GSCSPFLLDG
     THGYTCSCSP GYTGPLCKTT TTFSFERRGY LLLQSPLVDA NCNITLSFKT VLPRALLFQR
     NTRGLLLSLE LDGGQLRLTL RRVASAGAEA EILSQVLEIS QNVTDGEWHS VEAVLGNWLL
     SLKLLDDAGS CAGQSCHKVA PVQSTLAGFV SSPQSTFIGG IPQDSKGRSE HSALPAFIGC
     MRDVFVDWQL IVPEEWLSDS AINVSPGCSH RDRCLDVPCQ NRGQCVNLWQ SYQCRCPRPY
     EGQDCEEEHV TARFGNEDSH SYAAFTITED LGHNLSISLF LRTRRHSGLL LVFSNSSSQY
     LHMWLEDGRV TVQLNNYESV KSESTIDDAE VHFVNLEVAE GRMALHVAAE KQGDVEVRTV
     DVRAGDTVHV GGLLEKRSTA VFGGYFKGCI QDLRISDRRL QFFGLDTSVR SYPLELMENV
     TAGCSGDNAC SRNPCLNGGM CYSTWDDFTC TCPPNTSGRR CEEVRWCELS PCPTDAECRM
     LNQGYECYSN ATFLDDSTVL SYQGNGYISR NLTNLSLSLR TRKRNAAILH AEKSSAFITV
     SIQDGFLFME LQSTSEGVSP VSLSSRRSVS DGEWHSVHLF MAAPWAQTSR WSLVLDENIE
     EASTSKSEGG NLNFLRQGVD IFLGGLAPEA GWSLAGCLST VELGGIALSY LSSSDVNLPR
     LQEEQFTQTS LSPALLGCSG APVCEPNPCL NGGECQDLFN TYNCSCTEGW AGRRCDFFLD
     TCASNPCVHG NCSINGLTYE CICEFGYTGV DCEEDLDVCE NHLCAHGGTC LHGPDRYACL
     CPENYTGPLC NERVEEIPWY IVVKNVRPKL PVSVCGDDTR NYTCFNGGNC TNRELSCDCP
     PGFIGHRCEQ EVDECKSNPC LNGGYCRNLI DKFSCVCEMS FAGDLCQTDM TSDGLTSDLL
     LSISLVSVIM LLVLILTSVG LVVALNRRAT HGTYSPSRQE KEGSRVEMWS ITQPPPMERL
     I
//
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