ID A0A3R7PK84_PENVA Unreviewed; 1229 AA.
AC A0A3R7PK84;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE SubName: Full=Peritrophin 1 {ECO:0000313|EMBL:ROT74564.1};
GN ORFNames=C7M84_006899 {ECO:0000313|EMBL:ROT74564.1};
OS Penaeus vannamei (Whiteleg shrimp) (Litopenaeus vannamei).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Dendrobranchiata;
OC Penaeoidea; Penaeidae; Penaeus.
OX NCBI_TaxID=6689 {ECO:0000313|EMBL:ROT74564.1, ECO:0000313|Proteomes:UP000283509};
RN [1] {ECO:0000313|EMBL:ROT74564.1, ECO:0000313|Proteomes:UP000283509}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Muscle {ECO:0000313|EMBL:ROT74564.1};
RA Zhang X., Yuan J., Li F., Xiang J.;
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ROT74564.1, ECO:0000313|Proteomes:UP000283509}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Muscle {ECO:0000313|EMBL:ROT74564.1};
RA Sun Y., Gao Y., Yu Y.;
RT "The decoding of complex shrimp genome reveals the adaptation for benthos
RT swimmer, frequently molting mechanism and breeding impact on genome.";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
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:ROT74564.1}.
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; QCYY01001877; ROT74564.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3R7PK84; -.
DR Proteomes; UP000283509; 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 PANTHER; PTHR23301:SF0; LP10853P; 1.
DR Pfam; PF01607; CBM_14; 12.
DR SMART; SM00494; ChtBD2; 13.
DR SUPFAM; SSF57625; Invertebrate chitin-binding proteins; 13.
DR PROSITE; PS50940; CHIT_BIND_II; 12.
PE 4: Predicted;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Reference proteome {ECO:0000313|Proteomes:UP000283509};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 142..188
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000259|PROSITE:PS50940"
FT DOMAIN 276..331
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000259|PROSITE:PS50940"
FT DOMAIN 365..433
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000259|PROSITE:PS50940"
FT DOMAIN 464..519
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000259|PROSITE:PS50940"
FT DOMAIN 549..604
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000259|PROSITE:PS50940"
FT DOMAIN 635..690
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000259|PROSITE:PS50940"
FT DOMAIN 721..776
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000259|PROSITE:PS50940"
FT DOMAIN 807..862
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000259|PROSITE:PS50940"
FT DOMAIN 969..1023
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000259|PROSITE:PS50940"
FT DOMAIN 1056..1102
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000259|PROSITE:PS50940"
FT DOMAIN 1121..1161
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000259|PROSITE:PS50940"
FT DOMAIN 1180..1229
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000259|PROSITE:PS50940"
FT REGION 13..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 880..965
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..113
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 880..938
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 939..959
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1229 AA; 132954 MW; 59FC678CE7F9D003 CRC64;
MCSYNCGDSN NCRPDNNRRP DNNRRSDNDC RADNNRRSDN CRADNNPAPT TAAPTTTAAA
PPTTAAPTTT AAPTTTAAPT TTAAPTTTRR DNNCRSDNNR RSDNNRRSDN NRRSDNSTTA
ADTSVTEGNS ENICDCECCV KPHPTDCTAY YYCEPGHLAK YFTCTEGLVF HPEVRQCVLE
VQYPQCQVSS GDEDECDFTC PNAEGMYAHP RDCNKWHKAS CPLTNLVFNA AKKVCDWSEN
VECTSASDAE CVLTIVETVT DAPVTESNGD NTEDCDFVCP EVEGIYAHPR DCSKFVTCAN
SRPSTASCPP NLVFNAAKKV CDWSENVECT SASDAECVLT IVETVTDAPK VCDWSENVEC
TSASDAECVL TIVETVTDAP VTEVEGIYAH PRDCSKFVTC ANSRPSTASC PPNLVFNAAK
KVCDWSENVE CTSASDAECV LTIVETVTDA PVTEGNGDNT EDCDFVCPEV EGIYAHPRDC
SKFVTCANSR PSTASCPPNL VFNAAKKVCD WSENVECTSA SDAECVLTIV ETVTDAPVLK
NGDNTEDCDF VCPEVEGIYA HPRDCSKFVT CANSRPSTAS CPPNLVFNAA KKVCDWSENV
ECTSASDAEC VLTIVETVTD APVTEGNGDN TEDCDFVCPE VEGIYAHPRD CSKFVTCANS
RPSTASCPPN LVFNAAKKVC DWSENVECTS ASDAECVLTI VETVTDAPVT EGNGDNTEDC
DFVCPEVEGI YAHPRDCSKF VRCANSRPST ASCPPNLVFN AAKKVCDWSR NVECTSASDA
ECVLTIVETV TDAPVTEGNG DNTEDCDFVC PEVEGIYAHP RDCSKFVRCA NSRPSTASCP
PNLVFNAAKK VCDWSENVEC TSASDAECVL TIVETPTTTA APTTTALSAD RRSDNNDSAA
PTTTPAPTTK QPRSDNNPRS DNNPASDKTP APTTIRQQPP LRQQPPAPTT TPAPTTTPAP
TTTPSGECNF ACPEKGLYPH PRKCSEYVFC DNSVADVRQC PAGLHYNPTS KNCDWPQNVA
CSDNEEASCT LSNPTTPPRL PNPNKQICDC ECCLKAHPDD CTSYYYCAPG ADAQFFACSE
GLVFHPEFKQ CVLQTQYPQC QPEVPPTCDP TCECLYPSEI CSEYFKCNMQ GTPIKYECTG
GLVFNNNTYS CDFPRNVQCS ETRPKRSLTY DDAPQQYVTA EECKQLEGKF AVEGNASAYY
LCSHGTAHLM RCPDLAVFSS AAQDCIFMK
//