HEXA_ANOGA
ID HEXA_ANOGA Reviewed; 692 AA.
AC Q17020; O76209; O77461; Q17019;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 2.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=Hexamerin-1.1;
DE Short=HEX-1.1;
DE AltName: Full=AgHex-1.1;
DE AltName: Full=AgHexA;
DE Flags: Precursor;
GN Name=HexA;
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], DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX PubMed=9219531; DOI=10.1111/j.1432-1033.1997.t01-1-00719.x;
RA Zakharkin S.O., Gordadze A.V., Korochkina S.E., Mathiopoulos K.D.,
RA della Torre A., Benes H.;
RT "Molecular cloning and expression of a hexamerin cDNA from the malaria
RT mosquito, Anopheles gambiae.";
RL Eur. J. Biochem. 246:719-726(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Agbabilame;
RX PubMed=9755210; DOI=10.1093/genetics/150.2.807;
RA Caccone A., Min G.-S., Powell J.R.;
RT "Multiple origins of cytologically identical chromosome inversions in the
RT Anopheles gambiae complex.";
RL Genetics 150:807-814(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-667.
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 333-588.
RC STRAIN=Gasua;
RX PubMed=8807302; DOI=10.1093/genetics/143.3.1307;
RA della Torre A., Favia G., Mariotti G., Coluzzi M., Mathiopoulos K.D.;
RT "Physical map of the malaria vector Anopheles gambiae.";
RL Genetics 143:1307-1311(1996).
CC -!- FUNCTION: Larval storage protein (LSP) which may serve as a store of
CC amino acids for synthesis of adult proteins. {ECO:0000250}.
CC -!- SUBUNIT: Homohexamer. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000250}.
CC Note=Minor constituent of late larval hemolymph.
CC -!- TISSUE SPECIFICITY: Larval fat body. {ECO:0000269|PubMed:9219531}.
CC -!- DEVELOPMENTAL STAGE: First detected in fourth-instar larvae and
CC disappears abruptly in early pupae. {ECO:0000269|PubMed:9219531}.
CC -!- SIMILARITY: Belongs to the hemocyanin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA93477.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U51225; AAA96405.1; -; mRNA.
DR EMBL; AF020870; AAC31873.1; -; Genomic_DNA.
DR EMBL; AF020871; AAC31874.1; -; Genomic_DNA.
DR EMBL; AF020872; AAC31875.1; -; Genomic_DNA.
DR EMBL; AAAB01008960; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAAB01018287; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U50475; AAA93477.1; ALT_FRAME; mRNA.
DR AlphaFoldDB; Q17020; -.
DR SMR; Q17020; -.
DR PaxDb; Q17020; -.
DR VEuPathDB; VectorBase:AGAP005768; -.
DR eggNOG; ENOG502QR98; Eukaryota.
DR HOGENOM; CLU_012213_1_0_1; -.
DR InParanoid; Q17020; -.
DR Proteomes; UP000007062; Chromosome 2L.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0045735; F:nutrient reservoir activity; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1280.10; -; 1.
DR Gene3D; 1.20.1370.10; -; 1.
DR Gene3D; 2.60.40.1520; -; 1.
DR InterPro; IPR008922; Di-copper_centre_dom_sf.
DR InterPro; IPR013788; Hemocyanin/hexamerin.
DR InterPro; IPR000896; Hemocyanin/hexamerin_mid_dom.
DR InterPro; IPR005203; Hemocyanin_C.
DR InterPro; IPR037020; Hemocyanin_C_sf.
DR InterPro; IPR005204; Hemocyanin_N.
DR InterPro; IPR036697; Hemocyanin_N_sf.
DR InterPro; IPR014756; Ig_E-set.
DR PANTHER; PTHR11511; PTHR11511; 1.
DR Pfam; PF03723; Hemocyanin_C; 1.
DR Pfam; PF00372; Hemocyanin_M; 1.
DR Pfam; PF03722; Hemocyanin_N; 1.
DR PRINTS; PR00187; HAEMOCYANIN.
DR SUPFAM; SSF48050; SSF48050; 1.
DR SUPFAM; SSF48056; SSF48056; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS00210; HEMOCYANIN_2; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Reference proteome; Secreted; Signal; Storage protein.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..692
FT /note="Hexamerin-1.1"
FT /id="PRO_0000013337"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 9
FT /note="A -> E (in Ref. 1; AAA96405 and 2; AAC31873/
FT AAC31874/AAC31875)"
FT /evidence="ECO:0000305"
FT CONFLICT 186
FT /note="D -> N (in Ref. 2; AAC31874/AAC31875)"
FT /evidence="ECO:0000305"
FT CONFLICT 199
FT /note="V -> I (in Ref. 1; AAA96405 and 2; AAC31873)"
FT /evidence="ECO:0000305"
FT CONFLICT 225
FT /note="Y -> N (in Ref. 1; AAA96405 and 2; AAC31874/
FT AAC31875)"
FT /evidence="ECO:0000305"
FT CONFLICT 234
FT /note="C -> Y (in Ref. 1; AAA96405 and 2; AAC31873/
FT AAC31874/AAC31875)"
FT /evidence="ECO:0000305"
FT CONFLICT 325
FT /note="F -> Y (in Ref. 1; AAA96405 and 2; AAC31873)"
FT /evidence="ECO:0000305"
FT CONFLICT 480
FT /note="T -> A (in Ref. 2; AAC31873)"
FT /evidence="ECO:0000305"
FT CONFLICT 554
FT /note="F -> S (in Ref. 1; AAA96405 and 2; AAC31874/
FT AAC31875)"
FT /evidence="ECO:0000305"
FT CONFLICT 652
FT /note="S -> N (in Ref. 2; AAC31874/AAC31875)"
FT /evidence="ECO:0000305"
FT CONFLICT 683..684
FT /note="TE -> ND (in Ref. 2; AAC31873)"
FT /evidence="ECO:0000305"
FT CONFLICT 691
FT /note="R -> T (in Ref. 2; AAC31873)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 692 AA; 83495 MW; E8B5ADF2B5CB2FC6 CRC64;
MKLLILAVAI SLAVLASGSY VPSTKFEAKY ADKEFLFKQK FFFEVLRNIH LPLKYDEYIP
YTKTWVSDET KYNDFAQVAE FFDYYKTGAF LEKGELFSIY NEQYLRQTYA VFTFLYNSAD
WDTYYKNMIW ARDNINEGMF IYVLHLTVMH RPDLQGIVLP AIYEIYPYYF FNTDVIRTIN
YKKLYDPKFG FYGNGKYNVV YANYTATYPM DYYNNFYTEE YLNYYTEDIG LNACYYYFMM
DYSFLLGGDK FGLIKDRRGE LYWYMHQMLL ARYNLERMSN YMGTVKPLVW RFPLKTGYFS
LLSYWNGVPF KSRDYNYMIS DESYFKLDWI NAWEAKIRKI IEDGFFVKED GTRINLRLPE
SVEFFGNLLN SNVDSVDANY VGYIEVFSRL LLSGNDFNAY KVWPSALMQF ETSLRDPVFY
QLYERFMDLY YYFKRFLPSY TYEELNFNGV VIKDVTFDKL MTYFDYFDSD VSNVLPMQST
DKYFDYAVFA RQRRLNHKPF SYTMNVMSDY TGKAIIRAFV GPKFDRFFDL QFYKKYFFEI
DQYLVDFTAG KNTFVRNSRD FYWSVKDRTM YTDLYKKIML GYNGQEKFAL DMSEAHCGFP
DRLILPKGWT SGMPMQFYFI ITPYTAKTYE QGYQYDKTFT CGVESGMRFY DSLPFGYPFD
RVINFNYFYT KNMYFKDVFI FHTEEMKMNQ RY
