ID A0A091PKC3_APAVI Unreviewed; 1031 AA.
AC A0A091PKC3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Multiple epidermal growth factor-like domains protein 10 {ECO:0000313|EMBL:KFP91955.1};
DE Flags: Fragment;
GN ORFNames=N311_11834 {ECO:0000313|EMBL:KFP91955.1};
OS Apaloderma vittatum (Bar-tailed trogon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Trogoniformes; Trogonidae; Apaloderma.
OX NCBI_TaxID=57397 {ECO:0000313|EMBL:KFP91955.1, ECO:0000313|Proteomes:UP000054244};
RN [1] {ECO:0000313|EMBL:KFP91955.1, ECO:0000313|Proteomes:UP000054244}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N311 {ECO:0000313|EMBL:KFP91955.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; KL392080; KFP91955.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091PKC3; -.
DR Proteomes; UP000054244; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR CDD; cd00055; EGF_Lam; 1.
DR Gene3D; 2.10.25.10; Laminin; 1.
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; IPR002049; LE_dom.
DR PANTHER; PTHR24035; MULTIPLE EPIDERMAL GROWTH FACTOR-LIKE DOMAINS PROTEIN; 1.
DR PANTHER; PTHR24035:SF136; MULTIPLE EPIDERMAL GROWTH FACTOR-LIKE DOMAINS PROTEIN 10; 1.
DR Pfam; PF12661; hEGF; 6.
DR Pfam; PF00053; Laminin_EGF; 7.
DR PRINTS; PR00011; EGFLAMININ.
DR SMART; SM00181; EGF; 17.
DR SMART; SM00180; EGF_Lam; 14.
DR PROSITE; PS00022; EGF_1; 15.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 8.
DR PROSITE; PS50027; EGF_LAM_2; 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 Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Laminin EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00460};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000054244};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 755..780
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 37..72
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 80..115
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 179..209
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 182..223
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 217..252
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 392..427
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 478..513
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 614..644
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 652..687
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DISULFID 62..71
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 105..114
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 199..208
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 242..251
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 417..426
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 503..512
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 634..643
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 677..686
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP91955.1"
FT NON_TER 1031
FT /evidence="ECO:0000313|EMBL:KFP91955.1"
SQ SEQUENCE 1031 AA; 110047 MW; 77210677AE1E940B CRC64;
HCADKCVHGR CIAPNTCQCE PGWGGPNCSS ACDSDHWGPH CSSRCQCKNG ALCNPITGAC
HCASGFKGWR CEERCDQGTY GNDCHQKCQC QNGATCDHVT GECRCPPGYT GAFCEDLCPP
GKHGPQCEER CPCQNGGICH HVTGECACPP GWMIIFFLHT QGMVCGQPCT EGRYGKNCSQ
ECQCHNGGNC DSATGQCHCS PGYTGERCQD ECPVGTYGLQ CAETCKCMNG GKCYHISGAC
LCEPGYTGEH CETRLCPEGI YGLKCDKKCP CHMPNTWSCH PMSGECSCKP GWSGLYCNET
CSPGFYGKSC QQICSCQNGA DCDSVTGKCT CAPGFKGATC GTPCLPGTYG VNCSSVCNCK
NEAICSPVDG SCACKAGWHG VDCSINCPSG TWGLGCNLTC QCLNGGACNA LDGTCTCAPG
WRGEKCELPC QDGTYGMDCA ERCDCSHADG CHPTTGYCRC LPGWSGIHCD SVCAEGQWGP
NCSLSCYCKN GASCSPDDGI CECAPGYRGT TCQRICSPGF YGHRCSQTCP QCVHSSGPCH
HITGLCDCLP GFTGALCNEV CPSGRFGKNC IGICTCTNNG TCNPIDRSCQ CYPGWIGSDC
SQPCPPSHWG PNCIHTCNCH NGAYCSAYDG ECKCTPGWTG LYCTQRCPLG FYGKDCALIC
QCQNGADCDH ISGQCTCRTG FMGKHCEQKC PQGTYGYGCR QICDCLNNST CDHITGTCYC
SPGWKGARCD QAGVIIVGNL NSLSRTSTAI PADSYQIGAI AGIIILVLVV LFLLVLFIIY
RQKQKGKETN MPAVTYTPAM RVINADYTIS ETIPHSNGGN ANSHYFSNPS YHTLTQCTTP
PHVNNMDRLS LAKAKNNQLF VNLKNLEPGK RGTVLDYTGT LPADWKHGGY LNELGAFGLD
RGYLGKSLKD LVKNSEYNLS NCSLSSSENP YATIKDPPAL VPKSSECGYV EMKSPARRDS
PYAEIASSSS ANKNVYEVEP TVSVVQGAFS SSGRFSQDPY DLPKNSHIPC HYDLLPVRDS
PTSSTKEVSS E
//
