ID A0A091EEW2_CORBR Unreviewed; 1383 AA.
AC A0A091EEW2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Protein crumbs 1 {ECO:0000313|EMBL:KFO56503.1};
DE Flags: Fragment;
GN ORFNames=N302_00574 {ECO:0000313|EMBL:KFO56503.1};
OS Corvus brachyrhynchos (American crow).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Corvoidea; Corvidae;
OC Corvus.
OX NCBI_TaxID=85066 {ECO:0000313|EMBL:KFO56503.1, ECO:0000313|Proteomes:UP000052976};
RN [1] {ECO:0000313|EMBL:KFO56503.1, ECO:0000313|Proteomes:UP000052976}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N302 {ECO:0000313|EMBL:KFO56503.1};
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; KK718445; KFO56503.1; -; Genomic_DNA.
DR STRING; 85066.A0A091EEW2; -.
DR Proteomes; UP000052976; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR CDD; cd00054; EGF_CA; 14.
DR CDD; cd00110; LamG; 3.
DR Gene3D; 2.60.120.200; -; 3.
DR Gene3D; 2.10.25.10; Laminin; 16.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR013032; EGF-like_CS.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR001791; Laminin_G.
DR PANTHER; PTHR24049; CRUMBS FAMILY MEMBER; 1.
DR PANTHER; PTHR24049:SF1; PROTEIN CRUMBS HOMOLOG 1; 1.
DR Pfam; PF00008; EGF; 10.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF12661; hEGF; 4.
DR Pfam; PF02210; Laminin_G_2; 3.
DR PRINTS; PR00010; EGFBLOOD.
DR SMART; SM00181; EGF; 16.
DR SMART; SM00179; EGF_CA; 16.
DR SMART; SM00282; LamG; 3.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 3.
DR SUPFAM; SSF57196; EGF/Laminin; 10.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 11.
DR PROSITE; PS00022; EGF_1; 13.
DR PROSITE; PS01186; EGF_2; 9.
DR PROSITE; PS50026; EGF_3; 16.
DR PROSITE; PS01187; EGF_CA; 5.
DR PROSITE; PS50025; LAM_G_DOMAIN; 3.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000052976};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1321..1345
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 47..85
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 87..123
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 125..161
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 163..199
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 201..237
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 239..276
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 278..314
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 376..418
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 420..460
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 462..646
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 648..684
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 690..862
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 864..900
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 927..1114
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1116..1152
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1154..1189
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1191..1227
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1232..1272
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1274..1310
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DISULFID 56..73
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 75..84
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 113..122
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 151..160
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 189..198
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 227..236
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 450..459
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 674..683
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 890..899
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1142..1151
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1158..1168
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1179..1188
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1217..1226
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1262..1271
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1300..1309
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFO56503.1"
FT NON_TER 1383
FT /evidence="ECO:0000313|EMBL:KFO56503.1"
SQ SEQUENCE 1383 AA; 151192 MW; 40665B93DD2E1D70 CRC64;
SLCMRNDSRC LSNSCQKNST CVAGHKDDPC LCADASVDSV EELCNKTSNP CSSNPCLQNA
TCLGSAGNLS FTCECPAGYD GPTCDRADSA CDTNPCEHGG TCQSGLAGPS CLCRAGYTGT
LCEMDLDECT SEPCRNGALC RDGVDEYSCF CVPGYQGKHC DLEVNECASD PCLNGATCLN
QIGHYDCLCP LAYTGTNCEL EIDECLSQPC LNGGTCHDSL GSFSCSCTQG FLGDLCDTDI
DECSSQPCLH GGHCTDGANG YSCNCTGTGF MGLHCETLTP LCWSQPCYNN ATCEDHADNY
TCHCWPGAAL GRAPSRQQGT LTQPSSSPLA SDSVGQTQIL LMGNGRQMSD AIKLSQRNSL
ICVLKKTFTG THCDEDVNEC YTNPCQNGGI CENFPGNYTC HCPPADKEGI FYGGWNCTEV
LHGCTDHQCQ NNGICIPHLK NGQHGFSCIC SPGYTGMHCE TITTFSFQGN SFLLLKNPLT
HKKDFFYNIN LRFQTVQPTA FLFHRGEKDT FAKLELLNGY LHLSVQVNNQ PQALLRIPHN
VSDGEWHSVE VTLARAVILN LLDSSCVESC LNKTSAKIDN EPVMFAFQST FLGGLPVGNS
NPLQNTFNTH STPSFVGCLQ DIEIDLNVIT PENVSSGSSL NVRTGCAKKD WCDPHPCQNR
GRCINLWLSY RCDCYRPYTG PGCATEYIPG RFGSEDSSGY AAFPVDSTQN ENLIISMFVR
TRKPSGLLLA LRNSTYLYIR VYLEGGKLTM LALNSMKLLG KYSVNDGNFY LITLKIEPNK
MELFQSSHYL GFISTPTLTI QSKDILYIGG LPDKKETDRN GRYFKGCIQD VRVNNQPLEF
FPITNPLNSL INRTLINVTQ GCTGDNLCKS NPCHNGGVCY SIWDDFTCAC PPNTVGKACE
EVKWCELGPC PHEAQCQLVH QGFECLANAV FSGRSSAVFY RSNGKISRDL TNIIFGFRTR
DTDVILLYAE REPEFVVISI HNSKLLFQLQ SGNSFYRLTL ASSVPVSDGK WHQVMVSMVE
PLSQSSRWHM DIDNKKDTVT STAAAGSLNF LREETDIYVA DKAFDSLDGL RGCMSTIEIS
GIYLSYFENA DIPTKKPQEE QFLKISANPA FTGCLQVDFC SSDPCMHGGI CEDLYTSYHC
VCPDGWTGSY CEVNIDECSS NPCIHGNCTD GISSYGCSCE PGYTGENCEE DIDECHGHQC
VNGATCVDGV NGFSCLCAAN FTGRFCRYRR LPYTVCGNEE RNLTCFNYGN CTDLDGELTC
VCLPGFLGER CEKDIDECSS DPCLNGGLCQ NLLNKFHCLC DVNYAGDRCE IDLPADLISS
IFTSIGSVTL ALLVVLSLAM VVLAVTANKR ATQGTYSPSR QEKEGSRVEM WNMVQPPPME
RLI
//
