ID E2ADF6_CAMFO Unreviewed; 1704 AA.
AC E2ADF6;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Peritrophin-1 {ECO:0000313|EMBL:EFN68518.1};
GN ORFNames=EAG_09947 {ECO:0000313|EMBL:EFN68518.1};
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:EFN68518.1, 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GL438750; EFN68518.1; -; Genomic_DNA.
DR SMR; E2ADF6; -.
DR STRING; 104421.E2ADF6; -.
DR EnsemblMetazoa; XM_025414120.1; XP_025269905.1; LOC105251157.
DR InParanoid; E2ADF6; -.
DR OMA; PSKCIGT; -.
DR Proteomes; UP000000311; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0008061; F:chitin binding; IEA:InterPro.
DR Gene3D; 2.170.140.10; Chitin binding domain; 13.
DR InterPro; IPR002557; Chitin-bd_dom.
DR InterPro; IPR036508; Chitin-bd_dom_sf.
DR PANTHER; PTHR23301; CHITIN BINDING PERITROPHIN-A; 1.
DR Pfam; PF01607; CBM_14; 13.
DR SMART; SM00494; ChtBD2; 13.
DR SUPFAM; SSF57625; Invertebrate chitin-binding proteins; 13.
DR PROSITE; PS50940; CHIT_BIND_II; 13.
PE 4: Predicted;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Reference proteome {ECO:0000313|Proteomes:UP000000311};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..1704
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003157038"
FT DOMAIN 28..94
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000259|PROSITE:PS50940"
FT DOMAIN 616..675
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000259|PROSITE:PS50940"
FT DOMAIN 688..743
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000259|PROSITE:PS50940"
FT DOMAIN 753..812
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000259|PROSITE:PS50940"
FT DOMAIN 813..870
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000259|PROSITE:PS50940"
FT DOMAIN 923..982
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000259|PROSITE:PS50940"
FT DOMAIN 995..1049
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000259|PROSITE:PS50940"
FT DOMAIN 1059..1117
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000259|PROSITE:PS50940"
FT DOMAIN 1152..1210
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000259|PROSITE:PS50940"
FT DOMAIN 1271..1329
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000259|PROSITE:PS50940"
FT DOMAIN 1391..1449
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000259|PROSITE:PS50940"
FT DOMAIN 1522..1580
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000259|PROSITE:PS50940"
FT DOMAIN 1642..1700
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000259|PROSITE:PS50940"
FT REGION 95..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 868..931
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 868..919
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1704 AA; 184256 MW; AB843A8BDD00B2D6 CRC64;
MKEIYLVAIL YVATLSVALN ISSVTDFPTE CPAESQDKII YLPYENDCTK FYSCYMGIKG
EPQDCPFRDN KGNRLHFNPV LQVCDWPRSA GCKLSKPTSA SITPKSPPTS SSSSSSSPPT
VSSNSPISPT SSSNPPTTTS SSSSSTLPTS SSSSLPTTTS SSSPTSSSLP STISSDSPTS
PTSNPFPSAT PASSSPIFQS SSSLPPKTTL SSSSTSSISS STSSPETTTS NSPTSLTSPT
TPSSPTSSSS LPPKTTLSSS STSSISSSTS SPETTTSNSP TSLTSPTTPS SPTSSSLPST
ISSDSPTSPT SNPFPSTTSA SSSPILPSSS SLPPTTTLSS SSTSSTSSST SSPETTTSSS
PTSLTSPITP SSPTSSSSLP PTTTLSSSST SSTSSSTSSP ETTTSNSPTS LTSPTTPSSP
TSSSNPSTTT TSSSSPTSSS PPLTTSSDSS TSPTSSSSPF PPTTLSSNSP ASSTSPSSSP
LTSSSSTPIL PSSSSFPSIT TSSSSSLTSS SSSPIPTTTS SSPTSLTSNS PTTPSSSTLS
TSSSNPSTTT TSSSSPALPS SSPSTISSSS SPILPTSSSS LFPTMPSLPS SSISSTSTTI
STAISATTTE ISEKPRMQCP SESSTETVRI AHQCLCNVYY ECINGDKIRQ TCPIGMHFDY
EREVCDWPEA ANCVHSISTQ NFLIDRYENK CYQEGKAFQH EIDCSSYYLC VEGNKILKHC
MAGLHFNVTL QMCDYPTKAS CDFIVTFLPA ANPASCSSSN STEKVLLPHE CNCAQYYECI
NGNLLLQDCP NGLDFDRIRN TCSQPNDAKC PYVCPCASST KKVLLPHECN CGQYYECVRG
QPALRNCPNN LHFDYIEKIC KSSNEATCAT STKPTTTSTD STVTDTSITG STETDARITG
PTVTDTSITG STVTPTGGPE TPRQKCPPKG STEKARIAHP WVCYLYYECV NGNKEERMCP
IGKHFDYIQE VCDWPWKVNC MRPIPTHDMS IDDCHNKCSP EGRTFRHETD CSLYYLCSNG
KKILQQCTAG LHFNITLQIC NYPYKSCDLP DNTYSTITQN VCPSNSTEKI RFPHNCKCTY
YHECVNGKKI LHKCPEGLHF DIVQKTCNDP YKSGCAPTFP KSTPMPIIST TKWSKEPDKT
TTENPLDPSK CIGTCPEIDP PKAVLLPNED CKKFCMCSNG IAWVQPCPEP LYFDSKDTVC
KNKRDAVCGK RLFNQDRVSM HHRMFNENSL QSPKKENNDD QGIHDNSLSK HIYNFDDKTT
TENPLDPSKC IGTCPEIDPP KAVLLPNEDC KKFCMCSNGI AWVQPCPEPL YFDSKDTVCK
NKRDAVCGKR LFNQDRVSMH YRMFDEKNSL QSLNKENNDD HGIHDNSLSK HIYNFDDKTT
TENPLDPSKC IGTCPEIDPP KAVLLPNEDC KKFCMCSNGI AWVQPCPEPL YFDSKDTVCK
NKRDAVCGKR LFNQDRVSMH YRMFDEKNSL QSLNKENNDD HGIHDNSLSK HIYNFDDKTT
TDKTTTENPL DPSKCIDPSK CIGTCPEIDP PKAVLLPNED CKKFCMCSNG IAWVQPCPEP
LYFDSKDKVC KNKRDAVCGK RLFNQDRVSM YHRIFDEKNS LQTLKKENND DQGIHDNFLS
KHIYNFDDKT TTENPLDPSK CIGTCPEIDP PKAVLLPNED CKKFCMCSNG IAWVQPCPEP
LYFDSKDTVC KNKRDAVCGK RSFN
//