ID A0A2J7R7D1_9NEOP Unreviewed; 2282 AA.
AC A0A2J7R7D1;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Protein crumbs {ECO:0000313|EMBL:PNF36740.1};
GN ORFNames=B7P43_G11566 {ECO:0000313|EMBL:PNF36740.1};
OS Cryptotermes secundus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Polyneoptera; Dictyoptera; Blattodea; Blattoidea; Termitoidae;
OC Kalotermitidae; Cryptotermitinae; Cryptotermes.
OX NCBI_TaxID=105785 {ECO:0000313|EMBL:PNF36740.1, ECO:0000313|Proteomes:UP000235965};
RN [1] {ECO:0000313|EMBL:PNF36740.1, ECO:0000313|Proteomes:UP000235965}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Whole body {ECO:0000313|EMBL:PNF36740.1};
RA Harrison M.C., Jongepier E., Robertson H.M., Arning N., Bitard-Feildel T.,
RA Chao H., Childers C.P., Dinh H., Doddapaneni H., Dugan S., Gowin J.,
RA Greiner C., Han Y., Hu H., Hughes D.S.T., Huylmans A.-K., Kemena C.,
RA Kremer L.P.M., Lee S.L., Lopez-Ezquerra A., Mallet L., Monroy-Kuhn J.M.,
RA Moser A., Murali S.C., Muzny D.M., Otani S., Piulachs M.-D., Poelchau M.,
RA Qu J., Schaub F., Wada-Katsumata A., Worley K.C., Xie Q., Ylla G.,
RA Poulsen M., Gibbs R.A., Schal C., Richards S., Belles X., Korb J.,
RA Bornberg-Bauer E.;
RT "Hemimetabolous genomes reveal molecular basis of termite eusociality.";
RL Submitted (DEC-2017) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PNF36740.1}.
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DR EMBL; NEVH01006733; PNF36740.1; -; Genomic_DNA.
DR STRING; 105785.A0A2J7R7D1; -.
DR InParanoid; A0A2J7R7D1; -.
DR OrthoDB; 2877476at2759; -.
DR Proteomes; UP000235965; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IEA:UniProt.
DR GO; GO:0048513; P:animal organ development; IEA:UniProt.
DR GO; GO:0048468; P:cell development; IEA:UniProt.
DR GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR CDD; cd00054; EGF_CA; 27.
DR CDD; cd00110; LamG; 3.
DR Gene3D; 2.60.120.200; -; 4.
DR Gene3D; 2.10.25.10; Laminin; 34.
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:SF31; DELTA_NOTCH LIKE EGF REPEAT CONTAINING; 1.
DR Pfam; PF00008; EGF; 19.
DR Pfam; PF07645; EGF_CA; 3.
DR Pfam; PF12661; hEGF; 3.
DR Pfam; PF00054; Laminin_G_1; 2.
DR Pfam; PF02210; Laminin_G_2; 1.
DR PRINTS; PR00010; EGFBLOOD.
DR PRINTS; PR01983; NOTCH.
DR SMART; SM00181; EGF; 34.
DR SMART; SM00179; EGF_CA; 32.
DR SMART; SM00282; LamG; 4.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 4.
DR SUPFAM; SSF57196; EGF/Laminin; 20.
DR SUPFAM; SSF57184; Growth factor receptor domain; 4.
DR PROSITE; PS00010; ASX_HYDROXYL; 23.
DR PROSITE; PS00022; EGF_1; 29.
DR PROSITE; PS01186; EGF_2; 20.
DR PROSITE; PS50026; EGF_3; 34.
DR PROSITE; PS01187; EGF_CA; 8.
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:UP000235965};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..2282
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014423113"
FT TRANSMEM 2219..2242
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 33..195
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 197..233
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 236..276
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 280..316
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 318..355
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 357..393
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 395..431
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 433..471
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 472..508
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 512..544
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 545..581
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 583..619
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 621..657
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 659..697
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 699..735
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 737..773
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 775..812
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 814..850
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 852..888
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 890..927
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 929..965
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 967..1027
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1029..1064
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1066..1102
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1104..1145
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1147..1322
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1324..1360
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1367..1582
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1578..1614
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1891..1925
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1927..1963
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1965..2001
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2004..2042
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2045..2081
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2083..2125
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2127..2164
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2165..2205
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DISULFID 223..232
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 266..275
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 306..315
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 383..392
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 421..430
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 498..507
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 534..543
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 571..580
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 609..618
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 647..656
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 668..685
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 687..696
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 725..734
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 763..772
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 802..811
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 840..849
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 878..887
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 955..964
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1017..1026
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1033..1043
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1054..1063
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1092..1101
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1135..1144
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1350..1359
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1604..1613
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1915..1924
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1953..1962
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1991..2000
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2071..2080
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2154..2163
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2195..2204
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 2282 AA; 248096 MW; 9BE4BE05A5EE1A37 CRC64;
MSIYGSRCLS ASACLISVAL LLHTRNTISA QQSEGFFNGS SYVRLFSPIS LHGHTGLSFR
TCVGGELFSQ TNGGNSISLD VQTDRLLFSV MVQGQNFDTQ LNVRFLDNNW HTVNLLYRLG
NLTLSVMGHS QVVANSTYNS EVLNHPELSN ENSVLIVGKG FTGCLLEGPS IVFSRPLVQA
HNVEWGPCPH TINSCTKMDH CRNKPCLLHG ECISLPDRYE CKCAAGYSGN NCEINNGSPC
RRNNGNPCRN NGRCEEDAVG NYHCFCEGRF TGVHCETEIS SHLCESNPCQ NNGSCHVLDS
NYECTCLPGF TGQDCETNIN ECLPNPCLHG GNCVDGINNY TCLCGRTGYK GMKCEQNINE
CENNPCLNQG SCFDTYGSYT CQCMRGFGGQ NCELNLKECS SNPCRNGGVC KDSVGSYECQ
CFPGFTGTNC EVNINECEPG VCPADMECVD GVGTYQCVCR SGYPGTSLNC TGVGLCHSTP
CLNGGICTDL GDRYNCKCPA GFSGVHCERA SLLDWCIAVP CRNGGTCMGH SCECPPQFTG
HACETIVQCS TNPCQHSSKC LDYSDGYYCE CDPGWTGPNC ENDINECHSN PCRNAGTCVD
TINGFYCECA SGFTGNTCSV NIDECASGPC QNGGICIDHV HGYKCNCSED FMGDNCELEY
DVCGLLPCRN NGTCISIHNK RDYQCRCLSG FEGANCEVNI DDCVQASCPD NKVCIDGVND
YDCRCRQGFT GDNCTTSIDF CEDNPCQNNA TCANTYGNYT CICPVGISGR DCEHDIDECS
KSPEPCNNGI CVNSVGSYLC FCSPGFTGDH CDLDIDECLS QPCRNNATCE NRINSYHCVC
TPGFTGKDCG IDINECASVP CKNGATCIDD IAAFRCVCPP GLTGTLCEID IDDCEPLPCH
NDGVCVDGIN SFLCNCSDTG YEGYLCEKNI DDCLTAPCTN GAECHDGIKD YNCSCFEGYA
GKNCEIDIDE CESSPCQYGG TCLERSNQSL YRPAGSQPAL FPEKFNYMSA SGYKCVCVPG
ITGENCEINV NECDPEPCIH GSCKDVIGSY ECECEDGYEG TQCEIEIDEC ERYTPCVHGT
CSDRKANYYC DCEPKYGGKN CSVELTGCLD GPCLNNGTCK PYLENETNQK YNCSCPNGFH
GQNCTEVTTM SLNGSSLILV NTTREEGYDI QFRFKTTLSN GLLAIGKGST FYILELVHGK
LNLHSSLLNK WEGVFIGSKL SDSNWQKVFV AINSSHLVLA ANEEQTIYPI NLNEATNVSY
TSFPTTYLGG TLPYLSGLTH GPASFIGCTE DVVINGEWVL PNKHVKEAPY VPITLMGVEV
GCPREDQCKP NPCHNGGTCT DLWRNFTCAC ERPYLGHTCQ YNLTAATFGH ENITESLVTV
MVNDRARRSI RNVVDISMFI RTRQEDGTIF YLGSSSGIGS GEETFILAQL DAGELLVKIQ
FSGTLEKYTV GGQKLADGYN HLIQVVRNVT LVQVKMNGTE YFRKTISATG PLDVNVLYLG
GMPQMGRTIR QVEAIPDRSE ITKPPVNFKG IIQDVQISNG NRIMVVEFFP LGADDLEIPP
PFGTVSFDKT MVLEGVVSDN SCRSNPCEHS GTCFVTWNDF SCECPRGYKG KMCQEMEFCQ
LQNCPLGSTC QNLDNGYECI ANATFDGHNT SLSYSLHVTS NFSIKQLDTI SITYRSRTGG
TMLYINSGTE FFSVSVYNDE VTVAWKFNVM PLGQVYRFRK DEPDGNWTTV LIRMDNNGIM
GKFSFASEDT AQSFSASVFP LESWKKLVTS SKIILGGRAG VQDNIAFADG VSVSSKHSYV
TFGGEGFDTL GTGANENRVD YTSLPTVTTS ALPSALEGAF FKGCLGEVRI GGLLLPYFTP
DQLYSDNSST QDSFELSAPR KRVYDMESGC RLCFESECSN GGHCADPAES YVCNCSAGFE
GDGCTANINE CEQNRCENNA TCIDGIANYT CHCQQGWEGW LCDVDIDECT SNPCQHGGTC
INGLGKFECN CTDEYMGLYC ENFKLITCDN SPCLNGSTCT DVKNSKTGDN FTCTCMEGFV
GPVCNKPYCM EQPCQHGGTC DLTGVAPLCR CYPGYRGKYC EEDINECAEG PDKASPCKNG
ANCTDGINNY ICNCSGTGYK GLNCTEDIDE CTRDLFLCGA GSCVNIPGSF RCQCPEGKCG
SQCADDDPCS EKPCKNGGIC FEKCDSSPGD YYCECPVAFK GKNCTEMFAE EASHNAVDIA
IIVAPIVGLI LLVAAVGLSV FITMARKKRA TRGTYSPSQQ EYCNPRVEMD NVMKPPPEER
LI
//
