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Database: UniProt
Entry: A0A3P8SMF7_AMPPE
LinkDB: A0A3P8SMF7_AMPPE
Original site: A0A3P8SMF7_AMPPE 
ID   A0A3P8SMF7_AMPPE        Unreviewed;      2859 AA.
AC   A0A3P8SMF7;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Multiple EGF-like-domains 8 {ECO:0000313|Ensembl:ENSAPEP00000013623.1};
GN   Name=MEGF8 {ECO:0000313|Ensembl:ENSAPEP00000013623.1};
OS   Amphiprion percula (Orange clownfish) (Lutjanus percula).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Amphiprion.
OX   NCBI_TaxID=161767 {ECO:0000313|Ensembl:ENSAPEP00000013623.1, ECO:0000313|Proteomes:UP000265080};
RN   [1] {ECO:0000313|Ensembl:ENSAPEP00000013623.1, ECO:0000313|Proteomes:UP000265080}
RP   NUCLEOTIDE SEQUENCE.
RA   Lehmann R.;
RT   "Finding Nemo's genes: A chromosome-scale reference assembly of the genome
RT   of the orange clownfish Amphiprion percula.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSAPEP00000013623.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC       pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR   STRING; 161767.ENSAPEP00000013623; -.
DR   Ensembl; ENSAPET00000013986.1; ENSAPEP00000013623.1; ENSAPEG00000009579.1.
DR   GeneTree; ENSGT00940000160262; -.
DR   OMA; PVCQWCD; -.
DR   Proteomes; UP000265080; Chromosome 7.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0048513; P:animal organ development; IEA:UniProt.
DR   GO; GO:0042074; P:cell migration involved in gastrulation; IEA:Ensembl.
DR   GO; GO:0007368; P:determination of left/right symmetry; IEA:Ensembl.
DR   GO; GO:0055113; P:epiboly involved in gastrulation with mouth forming second; IEA:Ensembl.
DR   CDD; cd00041; CUB; 1.
DR   CDD; cd00054; EGF_CA; 1.
DR   CDD; cd00055; EGF_Lam; 3.
DR   Gene3D; 2.120.10.80; Kelch-type beta propeller; 4.
DR   Gene3D; 2.10.25.10; Laminin; 7.
DR   Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 2.
DR   InterPro; IPR000859; CUB_dom.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR024731; EGF_dom.
DR   InterPro; IPR011043; Gal_Oxase/kelch_b-propeller.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR015915; Kelch-typ_b-propeller.
DR   InterPro; IPR002049; LE_dom.
DR   InterPro; IPR002165; Plexin_repeat.
DR   InterPro; IPR016201; PSI.
DR   InterPro; IPR035914; Sperma_CUB_dom_sf.
DR   PANTHER; PTHR46093; ACYL-COA-BINDING DOMAIN-CONTAINING PROTEIN 5; 1.
DR   PANTHER; PTHR46093:SF17; MULTIPLE EGF-LIKE-DOMAINS 8; 1.
DR   Pfam; PF00431; CUB; 1.
DR   Pfam; PF12947; EGF_3; 1.
DR   Pfam; PF07645; EGF_CA; 1.
DR   Pfam; PF13415; Kelch_3; 1.
DR   Pfam; PF13418; Kelch_4; 2.
DR   Pfam; PF00053; Laminin_EGF; 4.
DR   Pfam; PF01437; PSI; 1.
DR   SMART; SM00042; CUB; 1.
DR   SMART; SM00181; EGF; 11.
DR   SMART; SM00179; EGF_CA; 2.
DR   SMART; SM00180; EGF_Lam; 4.
DR   SMART; SM00423; PSI; 9.
DR   SUPFAM; SSF57196; EGF/Laminin; 2.
DR   SUPFAM; SSF50965; Galactose oxidase, central domain; 1.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 2.
DR   SUPFAM; SSF117281; Kelch motif; 2.
DR   SUPFAM; SSF49854; Spermadhesin, CUB domain; 2.
DR   PROSITE; PS00010; ASX_HYDROXYL; 2.
DR   PROSITE; PS01180; CUB; 2.
DR   PROSITE; PS00022; EGF_1; 3.
DR   PROSITE; PS01186; EGF_2; 4.
DR   PROSITE; PS50026; EGF_3; 3.
DR   PROSITE; PS01187; EGF_CA; 2.
DR   PROSITE; PS01248; EGF_LAM_1; 3.
DR   PROSITE; PS50027; EGF_LAM_2; 2.
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   Kelch repeat {ECO:0000256|ARBA:ARBA00022441};
KW   Laminin EGF-like domain {ECO:0000256|ARBA:ARBA00023292,
KW   ECO:0000256|PROSITE-ProRule:PRU00460};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265080};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..2859
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018205685"
FT   DOMAIN          27..137
FT                   /note="CUB"
FT                   /evidence="ECO:0000259|PROSITE:PS01180"
FT   DOMAIN          168..201
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1086..1127
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1171..1218
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          1219..1269
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          1271..1412
FT                   /note="CUB"
FT                   /evidence="ECO:0000259|PROSITE:PS01180"
FT   DOMAIN          2131..2173
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DISULFID        27..54
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00059"
FT   DISULFID        172..182
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        191..200
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        1189..1198
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1241..1250
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1253..1267
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ   SEQUENCE   2859 AA;  311499 MW;  C75E836FA93EE575 CRC64;
     MASPLPVSFI LVVLLVAESP MCQAGDCKGH RQVFRGPPGY VTDGPGNYSV NGNCEWLIKA
     PSNSHRIVLN FTFMDTECTY DYLFVYDGDS YQSPLLASLS GNTLPQPIEA KSGKMLLHLF
     SDANYNLLGF NATYTFSLCP GACGGHGRCD SSTSKCHCHQ GWGGASCTTP LCAQACSVNG
     HCDKKGERCL CNPGFLGHSC QLGLHDDSGA GQWWHVSEGN PYTPPRTGSA GVYLSSTGAM
     YLFGGFDLNR ALGDLIKYNF TSNQWESRSY GHSPVARHSH TAVEYMGNMV IFGGELANGS
     LASDVWMYRP LQDDWQQLGF SHSHGAPRLA NHAAAVVDSY LYVFGGRTEE DMFSSTLYRF
     GLHGSGRWET VHPTGGKPPA TAGHSMVFHS PSRTLLVYGG HRPTTARFSV RVNNTDVFHV
     NRRFWTSFRS RFPATGPRER AFHSATVIGN YMVVYGGNVH IHYQEEKCYD EEIFLYHLGC
     HQWVSTGERC LRSMGGRYSH VAAVMEGRVL LVAGGYSGVA RGDLVAYKVP LFVSSDQGDR
     DAVCAEALDE SMCLKNPECS WCEGRCREYQ PTNPCGSTGC LGLARFLSDC QSCLVFSGTP
     PPLARAPGDF GWCVQNESCL PVSERSACRV DQISGAYGWW GERTLFLTSL HSCRTENYVP
     GLHLLTFQHP RNDSQPDKVS ILRSTTIILS PTTEMDVALQ FRGFIHPLWG GPPPAPPPTE
     TVSMWARIQR LHFDARMASG PNSSQLEVVG HWAAQQEKEL KLLARTDGSR LFSNLTRGNH
     YLVQAEGYLN NSGSGQTSEM ALIWNRTLPG GSEISFLFLE PYRSGSCSGY MSCLACLSDQ
     SCGWCPSLSR CLLRESPDLE PCPEVDKGDG KGEGQRHLLL APQHCTLCEE YRDCSACTQD
     PYCEWQINSS KKGDYQCSRR GRLDGSIRDS RGCPKVCNQR KTCGECLSNS SQCAWCESAQ
     ACFYFAAYLT KYPYGECRDW YDSVHSVPQC KQCSALNTCT DCLRTFQCGW CGDYNNPTIG
     KCLRGDWAGM DDPSVYNCSV AVAEARAANP EPQTSAPPRP LEMEMELEHL DDEEQDAIWS
     YPTCPDVEEC RLGLHNCHPF ATCINTPTSY ECHCERGYTG DGTLHCNQTC YNECREGQCS
     GSPRFECECS LGWTSDPATL VLSGVECDVD CGCNFHSTCI TAPGICDECQ DWTTGNHCEH
     CRPGSFGSAL AGGGGCVPCE CNGHGDPLRG YCHNQTGQCY CTHNTQGPHC ESCLPGYYGD
     PRNNGTCYRQ CQGRSVLLSS TSSSAMPLSS SLGWRSGTEG KGGLSHCLWV LSVTENLAPC
     LPRQFCPPVA LTLHPDSHTH CKSSYVYVFD GLPRFLGNGV VHSDHNLIGA FCGTTRTQPV
     TVEATSGVIS VYFEANVSSN KPQGFNASFW VRRCQQSSDE GEERSSVCPG GGQCQGGLCQ
     CPQGYGGPHC NRPMCPQDCG IAEGRGACNI SLGVCVCSDS WAGSDCSVPR DSNSLVWETL
     LDTQLTVNQA HRFLHRMGHS LVSGPQGNLW MYGGLSLSEG ILGNVYRYSV SEHRWTQMLT
     SSVEEGSTPG ARYHHASALL TSHDFGSGSY GASHNFMLVV GGVTQNGVAM DTWSLNLSSL
     VWREHKSTVL PPVAGHTLTV RRDASVLLIG GYSPENGFNH HLLEFNPHSG NWTVALHTGT
     PPTGLYGHSA VYHEQTDAIY VFGGYRFHVE TVEPSGELYS LYYPNLTWSL LVPSQGSKPL
     SRFFHAAALI KDTMVIVGGR TEAEDYSNSV SLYQINCNTW IQPASAVGDP VNRSVSLAMT
     SWGGRLFLSG GFNGVTLGRL LTLSVPSDPC ALLPTPEACN TTTGSCIWCR GTCASSDIAE
     RMGCFTGQSP CSPTPRQPDQ CRRLKTCSEC LARHPKTFSS SSQSALQCKW CTNCPEGACI
     SSSVSCTSEH DCRINQREIF LSSNCTETSC EASDCPKCTA SGKCMWTRQF KRTGETRRIL
     SVNPTYDWTC FSYALLNVSP MQVESSPPLP CPPPCHSLHN CSLCLGSRGS DGGWQHCVWS
     MTLQQCMSPS FVPLRCEAGQ CGRLLSGGDS CSPQCSQLTQ CSQCIARPQC GWCATRGGNG
     AGRCLQGGLD GVSEGVCPLR NSSWSFLHCP EEDECANGHH HCNSTQDCHD LSQGYHCTCK
     QGYILNSVSG QCEPVCAQGC VNGTCVSPGV CQCHFGFVGD NCSSQCSCNK HSNCAGVNKP
     DVCLECHNNT IGKHCEKCKP LFVGSAKGGG TCHPCREFCK GNSAVCLSRD EHKKALENPR
     LFPLDPNTIQ KWISEGPTED NAMCVNCQNN SVGDKCESCL SGYFLLQGKC EKCQCNGHAD
     TCNEHDGTGC PCQNNTETSS CLSSPQSDRK DCYRQQCAKC KDSFNGTPVN GRQCYRQFNV
     DTECCFDPTS QTNCFHFPTI RNLPKGRTVF FAAQPKFTNV DIRVTIDVTF GEVEVYVSNS
     HDTFIVDVDR YTGIHAIKIE EESVTRGTTT GVDKDSPPSP IKVFANASSS LGGPVLSHNP
     LQLQAKPSGS DREIREERAE GLITYITVWK PQTVLIVRGV RDRVVITFPH EVHSLKSSRF
     YIALRGVGTD EKQGESQGLL FLRQDQAHID LFVFFSVFFL QFLDFRREQR RHIQEMTKMA
     SRPFAKLTIY LEPEEPQLIY LPSAGGGVGG STVSLAHSRT SKLGGVVVGQ RGRAGAVSYK
     HDAGSGPTAH HHHHLTLGGG GNSGQHLPLH YLNTHHYAST TTGTPASHHH HPSTYSGYQH
     FCRSDPFLSQ LMGFSYSSFK VGPITLEPTD DGMAGVATVL FQLPGGVLAP NRACLGSALV
     TLRQNLQEYC GHGSGGGHPG VGAGRKGLLG HQHLTTMAM
//
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