ID A0A1I8PY21_STOCA Unreviewed; 2234 AA.
AC A0A1I8PY21;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Protein crumbs {ECO:0008006|Google:ProtNLM};
GN Name=106081592 {ECO:0000313|EnsemblMetazoa:SCAU012148-PC};
OS Stomoxys calcitrans (Stable fly) (Conops calcitrans).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Muscoidea;
OC Muscidae; Stomoxys.
OX NCBI_TaxID=35570 {ECO:0000313|EnsemblMetazoa:SCAU012148-PC, ECO:0000313|Proteomes:UP000095300};
RN [1] {ECO:0000313|EnsemblMetazoa:SCAU012148-PC}
RP IDENTIFICATION.
RC STRAIN=USDA {ECO:0000313|EnsemblMetazoa:SCAU012148-PC};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) 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 RefSeq; XP_013099114.1; XM_013243660.1.
DR EnsemblMetazoa; SCAU012148-RC; SCAU012148-PC; SCAU012148.
DR GeneID; 106081592; -.
DR VEuPathDB; VectorBase:SCAU012148; -.
DR OrthoDB; 2877476at2759; -.
DR Proteomes; UP000095300; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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; 17.
DR CDD; cd00110; LamG; 3.
DR Gene3D; 2.60.120.200; -; 4.
DR Gene3D; 2.10.25.10; Laminin; 27.
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:SF29; NEUROGENIC LOCUS NOTCH HOMOLOG PROTEIN 1; 1.
DR Pfam; PF00008; EGF; 14.
DR Pfam; PF07645; EGF_CA; 2.
DR Pfam; PF12661; hEGF; 6.
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; 27.
DR SMART; SM00179; EGF_CA; 24.
DR SMART; SM00282; LamG; 3.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 4.
DR SUPFAM; SSF57196; EGF/Laminin; 19.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 15.
DR PROSITE; PS00022; EGF_1; 23.
DR PROSITE; PS01186; EGF_2; 15.
DR PROSITE; PS50026; EGF_3; 27.
DR PROSITE; PS01187; EGF_CA; 7.
DR PROSITE; PS50025; LAM_G_DOMAIN; 4.
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}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 2171..2195
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 150..318
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 327..363
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 366..403
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 408..446
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 448..485
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 487..523
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 524..560
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 647..678
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 708..743
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 745..782
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 784..820
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 822..858
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 860..897
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 899..935
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 937..999
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1001..1037
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1039..1076
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1078..1119
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1121..1303
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1305..1341
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1348..1571
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1567..1603
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1632..1843
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1844..1878
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1880..1916
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1918..1954
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1957..1995
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1998..2035
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2037..2074
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2076..2114
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2115..2157
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DISULFID 353..362
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 393..402
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 417..434
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 436..445
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 513..522
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 550..559
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 668..677
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 733..742
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 772..781
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 810..819
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 848..857
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 925..934
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 989..998
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1027..1036
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1066..1075
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1109..1118
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1331..1340
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1593..1602
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1868..1877
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1906..1915
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1944..1953
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2025..2034
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2104..2113
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2147..2156
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 2234 AA; 244132 MW; 367B0CA902A73C9D CRC64;
MPSLILKPSS FSALLDLQQQ KNYHYHNQHL HCNQSQPRGE KQRRTTITKQ ISATSEPTKT
NLAMSATNIH TTTTTNTATT IKYASANHEQ NDSQLGATTN NIYSTNNKNN YSSTRSYRSL
TTTATTLPWL CCVLMFLLLS MESPFVAATS KEAYFNGSAY LRLLSPMPIW DHSAISFRSC
RGGEILAQQY NKNSIVISVI NDFLQISLAG PAVIGPNNRV DVKYSYHLLD NRWHTLQFKY
EYGNLLLFID RESRLFANST YNSQFLTNQD IGNEAAILIL GNSFTGCLQD GPGLQFINDS
MTVQNAVFGP CPLGSGPCSD HDIPLRNQDF CANDPCMGYG QCISHADGYE CRCTARYSGK
NCQMDNGSPC DRNPCSNGGT CFEDSRGDYQ CICNPNHTGK HCETEININP LCQINPCLNN
GACVVAAGSN SIECECPKGY TGSHCEIDMD DCASQPCQNN GKCVDKVNGF FCDCTNTGFL
GPLCQTNIDE CDMKPCRNGG KCFDTNGWYI CQCMEGWAGE VCEKPISCKT QQCLNGGTCI
DKQIGMHCLC PPGFSGELCQ QGPPPCPQCP IDSECVAGKC VCKPGTSEAS DSPASHENQV
VAVPQCNGGK SKRYIPPEWL KKKRCELKMS FNCEQPTTDV TSSIAAVGTG CKCLNGGTCS
LNGTHCYCPT GYSGDRCEKL EPCTLNNCQE PMICAQNKCI CPQDKVCTQC ASQPCRNGGM
CSDLPNGDYE CKCPAGWTGR NCVKDVDECA ISPKICGNGI CKNEEGSYKC YCTPGFTGIH
CDSDVDECLS HPCQNGATCH NKINAYKCVC PAGYKGLNCE IDIDECASNP CFNGSTCIDL
INNFTCSCIP GMTGRFCEID IDDCISGPCQ HNGICIDELG GFHCNCSSTG YEGRYCESNI
DECATNQCTN GAECIDQVND YFCKCFPGFR GKNCDIDINE CESNPCQFNG ICLERSNMTL
YALSQTMDLP SVFSQPFSFQ NASGYECVCV PGIVGKNCET NINECENNRC GKHGTCNDGI
GTYTCECDPG FEGTYCEINI DECDRYSPCG DHGTCIDQVN DYECDCDAMY GGKNCSVPLI
GCLSAPCSNG GICKPYLVNE TEHLFNCSCQ HGFQGYTCEK TTTISMVVSS LITVKTQREE
GYDINLQFRT TLPNGVLAFG TSGGQNEPVS YILELINGRL NLHSSLLNKW EGVFIGSNLN
DSNWHKVFVA INTSHLVLSA NDEQAIFPVG SYETSNGSQQ PSFPLTYLGG TIPNLKSYLR
HLTHRPSSFV GCMQDIVVNG KWIFPEEQGL DNDTKLTHIQ SGCPRTEQCN PNPCHSNGKC
TDLWHTFACT CQRPHFGYTC IYNITAATFG HENTTHSAVI VETNDVARRA IRSVLDISMF
IRTRQPTGQV FYLGSDPRKG KGADAGSSYV AAKLQGGELL VRMQFNGTPE AYTVGGNKLD
NGYNHLIEVV RNQTLVQVKL NGTEYFRKTL SSTGLLDAQV LYLGGPAPTT PPTEAPIVAG
SEVGTTEYAT IKPEDYFKGI IQDVKVSNGS HTMIVELYPL EEEDLALPPS FGTITIDRTS
VLKGEVSDDL CRKNPCRHNA ECRNTWNDYI CKCPNGYKGK DCQEIEFCQL VTCPGNSICQ
NLDDGGYECL TNITFRGNEK APLSFSFYKE PHLAEETKPK LKPVIEIAYR TRAGGTLLYL
ENQDSFFEIG VNQGQVTVTW KFNQDPLGDT KRFSKDNSDG IEWSRIFLRA QNGKLEGGWK
GWESMVDPSP SFSADIDIHA FEELISSGAQ VYLGGMPTES HQSRGTLSSQ QGSQFKGCLG
EARVGDLLLP YFTNDEMYPR TENVSVQPSV QFRLNSTRPD EGCILCFKSD CKNGGFCSSP
SESYACTCQA GYDGNDCSND IDECATAMCE NNSTCIDKVA DFFCSCLPGY DGRFCENNID
ECLDEPCHNG GNCTDLIAAF KCDCTDDYAG PQCDILKQVT CDNNPCKNGS TCQDKFNSQT
GNNFTCTCMQ GYEGPLCDTP FCEVKPCEHG GLCIISESRT PICQCSLGYT GPLCESDINE
CESNPCFNDG ICTDLVGGYS CNCTETGFEG DNCEIDIDEC AMSVEYCGGL GRCINLPGTF
KCICQDSFCG AYCNFTDPCK QSDVQLCMNG GTCQEACGDE ADYTCNCTDG YTGKNCTVLI
TAKEEPSTAD IAIIVIPVVV VLLLVCAGLL VTFLVMARNK RATRGTYSPS AQEYCNPRLE
MDNVLKPPPE ERLI
//
