ID A0A1I8QC63_STOCA Unreviewed; 1607 AA.
AC A0A1I8QC63;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 13-SEP-2023, entry version 40.
DE RecName: Full=Pikachurin {ECO:0008006|Google:ProtNLM};
GN Name=106080696 {ECO:0000313|EnsemblMetazoa:SCAU015798-PB};
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:SCAU015798-PB, ECO:0000313|Proteomes:UP000095300};
RN [1] {ECO:0000313|EnsemblMetazoa:SCAU015798-PB}
RP IDENTIFICATION.
RC STRAIN=USDA {ECO:0000313|EnsemblMetazoa:SCAU015798-PB};
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_013097617.1; XM_013242163.1.
DR RefSeq; XP_013097618.1; XM_013242164.1.
DR STRING; 35570.A0A1I8QC63; -.
DR EnsemblMetazoa; SCAU015798-RA; SCAU015798-PA; SCAU015798.
DR EnsemblMetazoa; SCAU015798-RB; SCAU015798-PB; SCAU015798.
DR GeneID; 106080696; -.
DR KEGG; scac:106080696; -.
DR VEuPathDB; VectorBase:SCAU015798; -.
DR OrthoDB; 2878505at2759; -.
DR Proteomes; UP000095300; Unassembled WGS sequence.
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:0030154; P:cell differentiation; IEA:UniProt.
DR GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR CDD; cd00054; EGF_CA; 2.
DR CDD; cd00110; LamG; 3.
DR Gene3D; 2.60.120.200; -; 3.
DR Gene3D; 2.10.25.10; Laminin; 2.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR001791; Laminin_G.
DR PANTHER; PTHR15036; PIKACHURIN-LIKE PROTEIN; 1.
DR PANTHER; PTHR15036:SF85; SP2353, ISOFORM A; 1.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF00054; Laminin_G_1; 3.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00282; LamG; 3.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 3.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS50025; LAM_G_DOMAIN; 3.
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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..1607
FT /note="Pikachurin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014271875"
FT DOMAIN 400..435
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 440..618
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 619..655
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 660..833
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1422..1607
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT REGION 216..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 300..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 880..986
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1019..1038
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1054..1160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1183..1397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 906..922
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 923..937
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 938..974
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1020..1038
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1054..1069
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1071..1085
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1095..1137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1140..1160
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1192..1208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1300..1326
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1327..1350
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1362..1378
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 404..414
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 425..434
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 645..654
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1607 AA; 179696 MW; 1ECA1E05384A5CE7 CRC64;
MKATKDNMLM HGFILVTILA TAKSAEAEIT MEAAFQGHCG HTSPCEQLCY EIHDGMYECD
CIEGYELNKN GYSCQVINST NSSDGHSKSD EDVLYQKGAS FSAKLANDNA DDNRLSSSYA
SSSAALASAL NRDSDEDLID GEDESAYISD DLGLLAHQQK VNSNDYYISN EGDDESLNSG
PERDIISDEY EDMAFERHQI AVTTARPLSL LLHRNRNAPS ASRGAAKPTK TLKAGGKTTT
VAKSPTTTAT TTTTTSTTES SFLNDNMDDL DDYYAKQDMS IYDDVNNNQL NLRPINHLTY
QQQQQEKRQL QQQQRHQTEA QISSRSNNRP QQPLYRNGNS NNSQKTATAA QNSPGAITNY
ATAASGTGTS SGGMGGAQGA KGVPEQQSAN ISYNLSSSET NEICNLECGM DGICERSEGT
SRCQCPFGKT GINCMEDIKV RVPKFSKHSW LAFPALKGAY KHVQLRIEFR PESFDGIILL
SGERDDLTGD FMALLLNKGF VEFWFDCGSG AGSVRSHETI LLNEWNSVVI YRHRWDAWLV
LNHGTKVQGR SNGLFSRITF REPVFLGGTG NITGLSNRLP ITVGFMGCIR HFMANDHEYK
FEEHPAGDVT KGFDIQDCIT DKCFKYPCQH GGKCLPSDQG AVCLCPIGFV GDLCEIRMDL
QVPSFNGSSF LRYAPLGDSV LIWLELKVIL KPEQADGLIL YSGPKHHGDF IALSLNNGYV
EFIFNLGNGP AVVRSEYPLS IGQWHSIRIS RTARLAVLKI DQMPEVMTIS SNGFWHLSLP
ENFFVGGVNH IDKLPMDLKS KPFFMGCIQR IEINGHPLSI ISEALGGTNI GNCPHACVAR
PCGPLSECVP QMESYECRCS AYNEQCKKAK KEMKADEDFD KNASKIQSKV PKTNKAGNAL
GRNELSAKDG KLHQMEQQPR GPKAHKKAKK QHMLWQHKQQ QHKVMQQQQK LRAATRTSNT
TPSTTTSTST TTTTTTTPPP PPSTTTTTMN WQDLDIINKD ILETQETLEH IMEKMKADDV
VLDDEEEDEV QDEDADEMED DMIFRDIKAM HEQQELEQQH EEEMERQKHL AWSSSGGSNS
NNLKSQRNRN KRKHSTAAST STSTTTTTTT TTTSTTTRTP STTKPFDMKS QYKQKQPQPY
DWKPDPHHKT PIMDKPQHKL SRLPTHYESF QTNTGSDILT FEDPIALEEQ WQDFNEPSSS
SSFESNEQIE GAQDKHETDT NVSINANDDV EDDDSVPANK DTPMENTSED TFVMDDTLFD
ESDGTEDYQR KQLAQDMKRI MANSKVPYTP KQPKLIITEY DYSNEEDHHN SQDTGSSDEE
NKERAKFQQT QPQQPVQQME IFQQSSLDDS TRRVSNDRDM GDADASEEDN VDEDNEDSQE
FVEIKKKPNS DPTQTHTDWS LLSKFDLPSN ENRPPIGVRK NFGACFVGHE SYFHYNDAET
MNQVISNNID LNLRIKTRSE RGVILWTACV GTMDQDSDDY LSLGIEDGFL HFRYNLGSGE
VDIRFNATKI SDGLWHRVRA IRNNQEGYLE VDGRKSITLR SPGTLRQLNT DTGLYVGGLP
DSVYFPRRRY TNGIVGCISE IVISGEFKMN FDPNTLGTAH NVETGIL
//
