ID E2A743_CAMFO Unreviewed; 1984 AA.
AC E2A743;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Contactin associated protein like 5-1 {ECO:0000313|EMBL:EFN70775.1};
GN ORFNames=EAG_04750 {ECO:0000313|EMBL:EFN70775.1};
OS Camponotus floridanus (Florida carpenter ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Formicinae; Camponotus.
OX NCBI_TaxID=104421 {ECO:0000313|Proteomes:UP000000311};
RN [1] {ECO:0000313|EMBL:EFN70775.1, ECO:0000313|Proteomes:UP000000311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C129 {ECO:0000313|Proteomes:UP000000311};
RX PubMed=20798317; DOI=10.1126/science.1192428;
RA Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA Wang J., Liebig J.;
RT "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT saltator.";
RL Science 329:1068-1071(2010).
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; GL437252; EFN70775.1; -; Genomic_DNA.
DR STRING; 104421.E2A743; -.
DR InParanoid; E2A743; -.
DR OMA; KCQNGAR; -.
DR Proteomes; UP000000311; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
DR CDD; cd00053; EGF; 1.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd00109; Kunitz-type; 1.
DR CDD; cd00110; LamG; 5.
DR Gene3D; 2.60.120.1000; -; 1.
DR Gene3D; 2.60.120.200; -; 6.
DR Gene3D; 2.10.25.10; Laminin; 2.
DR Gene3D; 4.10.410.10; Pancreatic trypsin inhibitor Kunitz domain; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR002223; Kunitz_BPTI.
DR InterPro; IPR036880; Kunitz_BPTI_sf.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR020901; Prtase_inh_Kunz-CS.
DR PANTHER; PTHR15036:SF49; AXOTACTIN; 1.
DR PANTHER; PTHR15036; PIKACHURIN-LIKE PROTEIN; 1.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF00014; Kunitz_BPTI; 1.
DR Pfam; PF02210; Laminin_G_2; 5.
DR PRINTS; PR00759; BASICPTASE.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00131; KU; 1.
DR SMART; SM00282; LamG; 6.
DR SUPFAM; SSF57362; BPTI-like; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 6.
DR PROSITE; PS00280; BPTI_KUNITZ_1; 1.
DR PROSITE; PS50279; BPTI_KUNITZ_2; 1.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS50025; LAM_G_DOMAIN; 6.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000000311};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1684..1705
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 19..69
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 140..335
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 336..374
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 378..564
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 560..740
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 964..1136
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1137..1174
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1194..1391
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1432..1632
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT REGION 92..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1641..1663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1712..1737
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1756..1893
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1649..1663
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1779..1818
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1819..1839
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1840..1889
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1984 AA; 223410 MW; 8EAB0031271A36CE CRC64;
MVEGTEDFTT IKKVLPDRCL AKIEQGPCTQ FVHKWYFNKT EGKCRTFPYG GCKGNDNRYN
SEDECLYYCV GGADHTLPPY LVTKGSVFVT TSGTTTTNSP LPTTSSTPRP TFTPPKPTKP
PVPKHKRGKE LTFMESGHEK TFMFAQSNTF IQLDGSGITT FQLRLCREIS FKFRTKLPHG
LLVYHSVKNR PEGLDPYALY VIVEKGQLKV VHVFGKQSTS LTVGEGLNRD EWHSVLVRID
VHGAKLIARV DDKKADTTLK VLERVVNYGV SEDLASVVLI GGLSSEERLH GVKYIIESFV
GCIRDMVLSS GKSASDLLPI RPLIATKHEN VKEGCIDKCR TRENLCFVPH QCVNHYNSLT
CDCFGTKYEG ERCDVYTATI LTLRGSSYVS FRVYDWKDRV HSSVNRISLA FKTKWDDSAL
FYASGEIDGT PHYIAASIIN GSVYVELDFG HNSKISTMLG DYVTSDHWNN LIISHNGSLV
FVSLDDEKKV LEVPGENYNM IIDPEIYIGG GPELHKKKGL LSHNNFAGSL KYVFFNDKSI
IYELKRSNPM VHYIGVLEPE YYEADVEVIP ITYPFAESHI WWPIERTDSL KLNFDFKSSK
PIAVVASGDI KSSRGVGYWE LRQVNDEIRF QLIPVITENI TVITSVKFPP YNTSWHAVEL
NYTKGDLNIL LDYKNKQSKF FALTFELGEK VIIGSGIIGS KSNAGLVGCM REIQVNNQRI
EPRYVINTER VIGEVALDNC QFVDPCKRPN TCEHGATYRK TCEELALLGF TQDDVYKIDI
DGNGRFPPAS VKCEFQSIED STKTIVEHNL PSQVDVRSIS ENDFSFNIKY RQFTAEMLQE
LISHSLYCSQ YVKYDCYKAP LELHSATWFL GSKGTTVDYI GNVNRGSCPC GMNRTCVNSN
LSCNCDVSAG NAGKWLSDEG YYETPDSLGI TGLIFLQQKD LEEDAQGRIT LGPLECVETN
TQKYVVTFTT SQSYIEVPGW RKGDIAFSFR TTGEKAILLY QPPIRNNYPS FMVALTSEYQ
LTFNFTLNTG TIRELEVRSR RKLNNGEWQK IWIDYNDYHV RFMINTDFQM VDLLSEEEFG
PFEGSMFIGG ATAEHLKTSS VRQGLIGCFR GLVVNGEILD IHSYMSVHLS EIIKDCKPSC
QPNKCQNGAR CVELWSNFEC VCENRWAHLG TFCETNINNK ALTFTSPGVF LKKNYFESDN
NEEKLQLKSM LQENILINLR TYDTHSLILY ANDHLNNFVH LYISNGTNIV YLFNAGNEIK
NITVSNPNVN TGISVQIAII RGENWTTLHV NEYNVTLNAV PILLDTYSNK PWTNPEKEVL
APQRPPAPPT DYFQVNLGGF DSNLLRVGQE GALIQGYVGC LRGLMIGKYL VDLPNLANEA
NHEGKGVLPN CQMKCDAMPC KNLGICTEDF NRQESSCNCE LTSYFGEYCA DEKGADFSGE
SVLQREFELE GEVNQVKVQL AFSTSELRQR TTALLLVQTD NKRSYYLLVA LTSEGQLIFE
EDRDGSAAYG VRLNDRNFLN GARHSVYYVR DNTTATLLID RQPAQLIPLP GLPIRVDEDE
TPGATEIQLG GLNTTDSRFI AYKGYTGCLS NVVISINGGP GMKPLEEYML FTKQASETVR
ATIPAGVRSA QCAVFHIQPG GLEPPRNVPN EGGDREWVED PPEKIPYKSQ YSSTTQEEQG
AGTYIFIALC CVFVVVVTGC IYEVWRSARK DRQRRHRAAS GAAATAASGS QRWQPPQYTE
SLVTTTGVKA VGFKNVMDDD KRPNGTHVKA LGAKEYKPLP NTEPKDLIND KNDKKVHIKA
DEESEKKELL GSMEDLREEP ELEEREEKEE EEEEEEDVQE QGTDKNKDQS QKQQQEEQEK
NEKNDQDNEP LVRPVRNKVA RRGSLTDELD PDDTQALLET NFSVTGLNEI KTERIIPRVN
NATKNITIPK RPMSLDLNAP IKFRKLRERA WPEKVTAKLL DGDEVSLQSR GRGYNDAAYR
TQDK
//
