ID A0A3B4TZK4_SERDU Unreviewed; 913 AA.
AC A0A3B4TZK4;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Multiple epidermal growth factor-like domains protein 11 {ECO:0000313|Ensembl:ENSSDUP00000011140.1};
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:ENSSDUP00000011140.1, ECO:0000313|Proteomes:UP000261420};
RN [1] {ECO:0000313|Ensembl:ENSSDUP00000011140.1}
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; A0A3B4TZK4; -.
DR STRING; 41447.ENSSDUP00000011140; -.
DR Ensembl; ENSSDUT00000011348.1; ENSSDUP00000011140.1; ENSSDUG00000008123.1.
DR GeneTree; ENSGT00940000155333; -.
DR OMA; PACNINC; -.
DR Proteomes; UP000261420; 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; 2.10.25.140; -; 1.
DR Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 6.
DR InterPro; IPR013032; EGF-like_CS.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR011489; EMI_domain.
DR InterPro; IPR002049; LE_dom.
DR InterPro; IPR042635; MEGF10/SREC1/2-like.
DR PANTHER; PTHR24043:SF9; PLATELET ENDOTHELIAL AGGREGATION RECEPTOR 1; 1.
DR PANTHER; PTHR24043; SCAVENGER RECEPTOR CLASS F; 1.
DR Pfam; PF12661; hEGF; 5.
DR Pfam; PF00053; Laminin_EGF; 6.
DR PRINTS; PR00011; EGFLAMININ.
DR SMART; SM00181; EGF; 17.
DR SMART; SM00180; EGF_Lam; 15.
DR PROSITE; PS00022; EGF_1; 14.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 11.
DR PROSITE; PS51041; EMI; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..913
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017200848"
FT TRANSMEM 844..867
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 18..96
FT /note="EMI"
FT /evidence="ECO:0000259|PROSITE:PS51041"
FT DOMAIN 138..168
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 176..211
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 219..254
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 267..297
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 305..340
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 442..472
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 480..515
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 566..601
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 654..689
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 702..732
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 783..818
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DISULFID 158..167
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 201..210
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 244..253
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 287..296
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 330..339
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 462..471
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 505..514
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 591..600
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 679..688
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 722..731
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 808..817
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 913 AA; 98031 MW; E5A542179D3ACE30 CRC64;
QTNSGVGFFV FILIISFLPR VLAFLSFSYA VTVQESYAHP FDQIYYTRCT DILNWFKCTR
HRISYKTAYR RGVRTMYRRR SQCCPGYFES GDLCVPLCTE ECVHGRCVSP DTCQCEPGWG
GLDCSSGCES DYWGPHCSNR CQCQNGAKCN PITGACVCTD GYQGWRCEEP CEYGYYGKAC
QLPCQCLNGA TCNHETGECI CAPGYTGAFC GERCPSGSHG PQCEQRCPCQ NGGTCHHITG
DCSCPAGWTG SVCAQPCPLG KYGINCSKDC SCRNGGLCDH ITGQCQCAAG FSGRRCQDDC
PVGTFGPQCN QRCECQNGAK CHHINGACLC ETGFKGPNCQ ERFCPPGLYG LICDKYCPCN
TTNTVSCHPL SGECTCSAGW TGLYCNETCP PGYYGEVCIL PCSCTNGADC HPVTGGCICA
PGFMGEDCAT VCPPGLYGPS CMSTCSCHNH ASCSPVDGSC ICREGWQGVD CSILCSSGTW
GLGCNQTCLC GNGAACDPMD GTCTCSPGWR GEHCDESCPD GTYGLECRER CDCTHANGCD
PVSGYCRCYP GWTGIHCDNV CPQGFWGPNC SVSCSCQNGG SCSPEDGTCV CAPGYRGTSC
KRICSPGFYG HRCSQSCPQC VHSTGPCHHV TGHCECLSGF SGSLCNQVCP SGRYGRACAE
ICLCTNNGTC NPIDGSCQCF PGWIGEDCSQ ACPSGHWGPD CLNSCNCHNG AQCSAYDGEC
RCSPGWTGLY CTQRCPSGFY GRDCSEVCRC QNGADCDHIT GQCACRTGFI GTSCEQKCPA
GTFGYGCQQL CECLNNATCD YVTGTCYCSP GYKGIRCDQA ALMMEELNPY TKISPARGSE
RQSAGAVMGI IFLLLIIMAM LSLFVWYRQR QRDKGHEIQP SVSYTQAMHI TNTDYSLSVA
RVHPDVLKSI RLM
//
