ID A0A3B4HC31_9CICH Unreviewed; 1055 AA.
AC A0A3B4HC31;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Multiple EGF like domains 10 {ECO:0000313|Ensembl:ENSPNYP00000031266.1};
OS Pundamilia nyererei.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Pundamilia.
OX NCBI_TaxID=303518 {ECO:0000313|Ensembl:ENSPNYP00000031266.1, ECO:0000313|Proteomes:UP000261460};
RN [1] {ECO:0000313|Ensembl:ENSPNYP00000031266.1}
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; A0A3B4HC31; -.
DR STRING; 303518.ENSPNYP00000031266; -.
DR Ensembl; ENSPNYT00000032018.1; ENSPNYP00000031266.1; ENSPNYG00000023573.1.
DR GeneTree; ENSGT00940000157703; -.
DR Proteomes; UP000261460; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 5.
DR InterPro; IPR013032; EGF-like_CS.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR013111; EGF_extracell.
DR InterPro; IPR002049; LE_dom.
DR InterPro; IPR042635; MEGF10/SREC1/2-like.
DR PANTHER; PTHR24043:SF8; EGF-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24043; SCAVENGER RECEPTOR CLASS F; 1.
DR Pfam; PF07974; EGF_2; 1.
DR Pfam; PF12661; hEGF; 5.
DR Pfam; PF00053; Laminin_EGF; 4.
DR PRINTS; PR00011; EGFLAMININ.
DR SMART; SM00181; EGF; 16.
DR SMART; SM00180; EGF_Lam; 13.
DR PROSITE; PS00022; EGF_1; 15.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 11.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 805..828
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 135..165
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 173..208
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 216..251
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 264..294
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 302..337
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 391..426
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 482..512
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 563..598
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 606..641
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 664..694
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 702..737
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DISULFID 155..164
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 198..207
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 241..250
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 284..293
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 327..336
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 416..425
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 502..511
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 588..597
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 631..640
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 684..693
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 727..736
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1055 AA; 113476 MW; 7D7874AEDD8FF419 CRC64;
EIEILQQDFE LSLVCLFFLS KTKEIGLDLR NCCCSQRDSY SVTVQESYAH SFNQIYYTSC
TDILNWFKLK KKKKKLSVKT ACSHGGKSWE KTVNVPQDCI HGRCMAPNTC QCEPGWGGSN
CSSACDNDHW GSHCSNRCQC QNGALCNPIT GACICTPGYR GWRCEVSCAV GTYGNGCQQK
CQCQNGAACH HATGECKCPP GYTGALCEEL CPPGKHGQQC EERCPCQNGG VCHHVTGECS
CPAGWMGTVC GQPCPEGRFG KNCSQECQCH NSGVCVSSTG QCICSPGYTG ERCQDECPLG
TYGAACAKTC NCENNSKCYH SNGMCLCEPG YTGKTCDVRL CPEGIYGLRC DRKCPCYVQS
TRGCHPISGE CTCLPGWSGL YCNETCTPGF YGESCQQVCQ CQNGADCHSV TGECICAPGF
TGPICSVPCP AGTFGVNCSS SCNCKNKAKC SPIDGSCSCK PGWHGLDCSI NCPSGTWGLG
CGSACICGNG GACNPLDGHC TCAPGWRGER CELHCQDGTY GLDCKERCDC NHADGCHHAT
GHCRCLAGWT GIHCDSVCAE GHWGPNCSLP CNCKNGASCS PDEGTCECAP GYRGPTCQRM
CPSGRFGKKC AQSCSCTNNG TCHPIDGSCQ CYPGWIGSDC SQCGFTLEII IYSCPTGHWG
PNCIHTCNCH NGAYCSAYDG ECKCSPGWTG LYCTQRCPLG FFGKDCSQTC QCRNGADCDH
ISGQCTCRTG FMGKYCDQKC PPGLYGYGCH QVCDCLNNST CDHMTGSCYC NSGWKGARCD
QAGVIVVGSL NTLTSAAMHV DSYQIGAIAG IIILVLLVLF LLLLFIIFRK KQKGKEPTMP
SVTYTPAVSV AADYNITATC EPHLSNYFSN PSYHTLTQCI SPQRGPNGKA KNNQVFVNVK
NMDQRKCALL ADHTGTLHAE WKHGDCLNQL DLMKGTPYHA SSCSLSSSEN PYATIKDPPM
LITKNTECGY VEMKSPARRD SPYAEISSRS PTNNQNVYEI DSTVSTIQST RDGSGLVKFG
QDPYDLPRNS HIPCHYDILP SRESPSSELK KLDSE
//
