ID   PE1_ANOGA               Reviewed;         153 AA.
AC   O76217; Q6VAW1; Q6VAW2; Q6VAW4; Q6VAW5; Q6VAW6; Q7QID7;
DT   11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 2.
DT   27-MAR-2024, entry version 112.
DE   RecName: Full=Peritrophin-1;
DE   AltName: Full=AgAper-1;
DE   AltName: Full=Peritrophic matrix protein 1;
DE   AltName: Full=Peritrophin A;
DE   Flags: Precursor;
GN   Name=Aper1; ORFNames=AGAP006795;
OS   Anopheles gambiae (African malaria mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=7165;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC   STRAIN=G3; TISSUE=Midgut;
RX   PubMed=9651363; DOI=10.1074/jbc.273.28.17665;
RA   Shen Z., Jacobs-Lorena M.;
RT   "A type I peritrophic matrix protein from the malaria vector Anopheles
RT   gambiae binds to chitin. Cloning, expression, and characterization.";
RL   J. Biol. Chem. 273:17665-17670(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Abraham E.G., Donnelly-Doman M., Fujioka H., Ghosh A., Moreira L.,
RA   Jacobs-Lorena M.;
RT   "Anopheles peritrophic matrix protein-1 (AgAper-1) regulatory sequences
RT   mediate transgenic protein accumulation and secretion into the midgut lumen
RT   upon blood ingestion.";
RL   Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=4aRR, L3-5, L3-51, Yaounde Yd21, Yaounde Yd35, and Yaounde
RC   Yd41;
RX   PubMed=15642974; DOI=10.4269/ajtmh.2004.71.795;
RA   Morlais I., Poncon N., Simard F., Cohuet A., Fontenille D.;
RT   "Intraspecific nucleotide variation in Anopheles gambiae: new insights into
RT   the biology of malaria vectors.";
RL   Am. J. Trop. Med. Hyg. 71:795-802(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PEST;
RX   PubMed=12364791; DOI=10.1126/science.1076181;
RA   Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R.,
RA   Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R.,
RA   Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z.,
RA   Kraft C.L., Abril J.F., Anthouard V., Arensburger P., Atkinson P.W.,
RA   Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C.,
RA   Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K.,
RA   Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V.,
RA   Dana A., Delcher A., Dew I., Evans C.A., Flanigan M.,
RA   Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R.,
RA   Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J.,
RA   Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I.,
RA   Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A.,
RA   McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D.,
RA   O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H.,
RA   Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J.,
RA   Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B.,
RA   Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M.,
RA   Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I.,
RA   Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J.,
RA   Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M.,
RA   Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C.,
RA   Collins F.H., Hoffman S.L.;
RT   "The genome sequence of the malaria mosquito Anopheles gambiae.";
RL   Science 298:129-149(2002).
CC   -!- FUNCTION: Binds chitin but not cellulose. May be involved in the
CC       spatial organization of PM. {ECO:0000269|PubMed:9651363}.
CC   -!- TISSUE SPECIFICITY: Adult peritrophic membrane.
CC       {ECO:0000269|PubMed:9651363}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in adult but not larval guts, whole
CC       pupae or whole bodies minus gut.
CC   -!- PTM: Glycosylated.
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DR   EMBL; AF030431; AAC39127.1; -; mRNA.
DR   EMBL; AY750997; AAV31069.1; -; Genomic_DNA.
DR   EMBL; AY344823; AAR02434.1; -; Genomic_DNA.
DR   EMBL; AY344824; AAR02435.1; -; Genomic_DNA.
DR   EMBL; AY344825; AAR02436.1; -; Genomic_DNA.
DR   EMBL; AY344826; AAR02437.1; -; Genomic_DNA.
DR   EMBL; AY344827; AAR02438.1; -; Genomic_DNA.
DR   EMBL; AY344828; AAR02439.1; -; Genomic_DNA.
DR   EMBL; AAAB01008807; EAA04177.3; -; Genomic_DNA.
DR   RefSeq; XP_308952.3; XM_308952.3.
DR   AlphaFoldDB; O76217; -.
DR   SMR; O76217; -.
DR   STRING; 7165.O76217; -.
DR   CAZy; CBM14; Carbohydrate-Binding Module Family 14.
DR   GlyCosmos; O76217; 1 site, No reported glycans.
DR   PaxDb; 7165-AGAP006795-PA; -.
DR   GeneID; 1270270; -.
DR   KEGG; aga:AgaP_AGAP006795; -.
DR   CTD; 1270270; -.
DR   VEuPathDB; VectorBase:AGAP006795; -.
DR   eggNOG; ENOG502R6AT; Eukaryota.
DR   HOGENOM; CLU_1682355_0_0_1; -.
DR   InParanoid; O76217; -.
DR   OrthoDB; 3680213at2759; -.
DR   Proteomes; UP000007062; Chromosome 2L.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR   Gene3D; 2.170.140.10; Chitin binding domain; 2.
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; 2.
DR   SMART; SM00494; ChtBD2; 2.
DR   SUPFAM; SSF57625; Invertebrate chitin-binding proteins; 2.
DR   PROSITE; PS50940; CHIT_BIND_II; 2.
PE   2: Evidence at transcript level;
KW   Chitin-binding; Disulfide bond; Glycoprotein; Reference proteome; Repeat;
KW   Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..153
FT                   /note="Peritrophin-1"
FT                   /id="PRO_0000023612"
FT   DOMAIN          18..79
FT                   /note="Chitin-binding type-2 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT   DOMAIN          92..153
FT                   /note="Chitin-binding type-2 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT   CARBOHYD        63
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        56..69
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT   DISULFID        130..143
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT   VARIANT         7
FT                   /note="L -> V (in strain: 4aRR, PEST)"
FT   VARIANT         19
FT                   /note="D -> V (in strain: 4aRR, PEST)"
FT   VARIANT         28
FT                   /note="E -> K (in strain: L3-5)"
FT   VARIANT         37
FT                   /note="P -> S (in strain: L3-5)"
FT   VARIANT         55
FT                   /note="K -> Q (in strain: Yaounde Yd41)"
FT   VARIANT         73
FT                   /note="A -> S (in strain: Yaounde Yd21, Yaounde Yd35,
FT                   Yaounde Yd41)"
FT   VARIANT         88
FT                   /note="A -> V (in strain: G3)"
FT   VARIANT         89
FT                   /note="P -> S (in strain: 4aRR, PEST)"
SQ   SEQUENCE   153 AA;  16791 MW;  2207D5130F487338 CRC64;
     MKVSASLVLL LAAAVLADDR CPPQDDPEQP PVLLAHPTDC DKFLICNHGT PVVSKCPPGL
     LWNDSQKQCD YPAQAQCAPG VTPNTEPAPK PSPNCPPEYD PDHMVYIPHE TDCGKYYICD
     PYGVELEQTC PSGLHWNPVV NYCDFPELAQ CEE
//