ID A0A3B3QB73_9TELE Unreviewed; 2831 AA.
AC A0A3B3QB73;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Multiple EGF-like-domains 8 {ECO:0000313|Ensembl:ENSPKIP00000003413.1};
GN Name=MEGF8 {ECO:0000313|Ensembl:ENSPKIP00000003413.1};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000003413.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000003413.1}
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR STRING; 1676925.ENSPKIP00000003413; -.
DR Ensembl; ENSPKIT00000027374.1; ENSPKIP00000003413.1; ENSPKIG00000020889.1.
DR GeneTree; ENSGT00940000160262; -.
DR Proteomes; UP000261540; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
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; 2.
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; 1.
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; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR006652; Kelch_1.
DR InterPro; IPR002049; LE_dom.
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; PF01344; Kelch_1; 1.
DR Pfam; PF13415; Kelch_3; 1.
DR Pfam; PF13418; Kelch_4; 1.
DR Pfam; PF00053; Laminin_EGF; 3.
DR SMART; SM00042; CUB; 1.
DR SMART; SM00181; EGF; 12.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00180; EGF_Lam; 4.
DR SMART; SM00423; PSI; 8.
DR SUPFAM; SSF57196; EGF/Laminin; 3.
DR SUPFAM; SSF117281; Kelch motif; 2.
DR SUPFAM; SSF103575; Plexin repeat; 1.
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; 5.
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; 1.
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|PROSITE-ProRule:PRU00460};
KW Lectin {ECO:0000256|ARBA:ARBA00022734}; Membrane {ECO:0000256|SAM:Phobius};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..2831
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017286474"
FT TRANSMEM 2569..2591
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 25..134
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 132..165
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1078..1119
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1208..1258
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1256..1400
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 2101..2142
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 2443..2488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 25..52
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00059"
FT DISULFID 136..146
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 155..164
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1230..1239
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1242..1256
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ SEQUENCE 2831 AA; 309257 MW; 75E26BD799D82363 CRC64;
MAGWLSPLLM VLLWAWVSSS QAGDCKGQRQ VLRGPPGYVT DGPGNYSVNG NCEWLIKPSS
SYSIVLNFTF METECTYDYL FVYDGDSYRS PLLASLSGTT LPQPIEAKSG KMLLHLFSDA
NYNLLGFNAT YSFSVCPGAC SGHGRCDTLS AHCLCPEGWG GPDCSSPLCP HVCPLHGSCD
KKGERCLCSS GFVGQSCQLG LRDDSGAGQW WEVSGGDANT PRRTAAAGVY LPSTEAMYLF
GFDLNKALGD LVKYNFTSNQ WEEVQHMVTP AARHSHTAVE WQGKMLVYGG ELANGSLAGD
IWMYRPLEDR WEQFGRGDLP GAPLLANHAA AVVDGYLYIF GGRTPEDMFS SILYRFDLRK
HQWEVVHPSG GKPPATAGHS MVFHRPSRTL LVYGGHRPTT ARFSVRVNST DMFHLDRRFW
TSLRSRFPAN GPRERAFHSA TVIGNYMVVF GNVHIHYQEE KCYDEDIFFY HLGCHQWVTG
GVDPIQGGIV RGRYSHVAAV MEGRLLLVAG GYSGIARGDL LAYKVPLFVS SDPGDRQDAV
CAEAPDESSC LKNPECSWCE GRCREYQPTD PCGSTGCLGL ARFLSDCQSC LVFSGSPASL
PRAPGDFGWC VQNESCLPVS QSACRVDQIS GAYGWWGERT RFLTFFNSCR AENFVPGMHL
LTFQHPRNNS QPDKVSILRS TSITLSPSTE MDVTLQFRGF IHPLWGSPPP APPTTETVSM
WARIQRLHFM ARMAAGPNSL KLSDVIGRWG AQQEKESHLL ARPSGFRLFQ NLTRGNRYLV
AAEGYLNNSG SGHTSEMALT WNRTVFPGGS EISFLFLEPY RSSSCSEYYS CLACLSDQSC
GWCPPQNRCL LRTSVEPCLE MSGELERHLL ITPQHCTLCE DYRDCAACTQ PQDPYCEWQI
SSSKKGDYQC SRRGRLEGSI RDSQGCPKVC NRTCGECLSN ASQCAWCESA QVCFYFAAYL
TKYPYGECRD WYDSVHSTPQ CKQCPALSTC TECLQTFQCG WCGDYDNPTI GCLRGDWAGL
ADDSAFNCSI AVAEVKAAPE PQTSSPPRIT EMELELEHLE GLLEGHKEAV WSYPSCPDVE
ECRLGLHRCH PFATCVNTAT AYECHCERGY TGDGVLHCNQ SCFNECREGR CSGSPRFECE
CALGWTSDPS TLVLSGVECD VDCGCNFHST CVTAPGICDQ WTSGLQCEQC RPGSFGSALA
GGEGCVPCQC NGHGDPLRGY CHNQTGLCYC THNTQGPQCE SCLPGFYGDP RNNGTCFRQC
QGRSVLLSSP SSQSPLLSAS LGWRGGAGAQ GGLSHCLWVL SVSKDLSPCL PGKQCPPVSL
MLHPDSRTPC PSSYVYVFDG LPRFLGNGVV QSDHNLIGAF CGTTRTMPVT VEATSVISVY
FEANVSSGPP QGFNASFWVQ RCQEGLLEDN TPCQGRAECR EGLCHCAKGY GGPHCDRLLC
PADCGSKEGR GMCVTALGIC QCSEGWAGPD CASPAGVNSL LWDNLLDTQM MANQAHRFLQ
RMGHSMVPGP QGTLWMYGGL SLTEGMLGNV YYSVSERRWT QMLTSIVEDG SAPSPRYHHA
SALLTSQESL AGTQGVMHGV MLVVGGVTQK GVAMDTWALN LSSLVWKEFK SSTLPPVAGH
TLTMRRSTTA LLIGGYSPEN GFNHQLLEFS LDSGNWTVAA HAGTPPTLYG HSAVYHEQTD
AVYVFGGYRF HVESVEPSGE LYSLYYPNLT WSLLVPSQGN KPLSRFFHAA ALLKDTMVVV
GGRTGEEDYS NSVSLYQINC NTWIQPLAVG EPVNKSVSLA MVAWEGHLFL SGGFNGVTLG
RLLTLSVPAD PCGLLPTSEA CNATTGSCVW FRGSCTSSDT AECSPTPRLP DQCRRLKTCS
ECLARHPKTF SNSAQLALQC KWCTNCPEGA CINSSVSCTS EHDCRINQRE IFLSSNCTET
SCEASDCPKC TASGKCMWTR QFKRTETRRI LSVNPTYDWT CFSYALLNVS PMQVESSPPL
PCPPPCHHLG TCSLCLGSRG SDGGWQQCVW SVALQQCMSP SFVPLRCEAG QCGRLLTRGD
SCSPQCSQLT QCSQCIARPQ CGWCATRGGN GAGRCLHGGL EVSEDVCPQW NSSWSFLHCP
EEDECANGHH HCNSTQDCHD QPQGYNCTCR QGYVLSVSGQ CEPVCSQGCV NGTCVSPGVC
RCHFGFVGDS CSAQCRCNKH SDCASLTQPD VCLECHNNTM GQHCEKCKPL FVGSALGGGM
CQPCRKFCQG NSAVCLSREE HKQALEHPRE FPLDPESWVM EGPTEVSAVC VNCQNNSVGD
KCETCLSGYF LLQGKCECQC NGHADTCNEH DGTGCPCQNN TETASCLTSS QSDRKDCYKQ
QQCAKCKDSF NGTPVNGRQC YRQFNVDHEC CFDPTSQSNC FHEPNIRNLP RGRTVFFAAQ
PKFTNVDIRV TIDVTFGEVE VYVSNSHDTF IVEVNRQTGV HSVKIEDDAP RGEVPPSPIK
LYTNSSTGLS PPPLPSTPLQ LQAKSPAAER EIREERAQGL ISYITVWKPQ TVLIVRGVRD
RVVITFPHEV HSLKSSRFYI VLRGVGTEAH DGQSQGLLFL RQDQAHIDLF VFFSVFFSCF
FLFLSVCVLL WKVKQFLDFR REQRRHIQEM TKMASRPFAK LTVYLEPEEP QLIYLPSCGM
PGGPISISHA RTGKLGGVMM GPRGRPGGVS YKHDPASGPA GHQLHHLSLS GGNSGQHLPL
HYLNTQHYAP TLAGTPSSHL QHHPSSHSGY QHFCRSDPFL SQLLGFSYSS FKVGPITLEP
TDDGMAGVAT LLIQLPGGIL APNRACLGSA LVTLRQNLQE YCGHGSGGAH PGAGGGRKGL
LGHQHLTTMA M
//
