ARY_ANTPE
ID ARY_ANTPE Reviewed; 704 AA.
AC Q7Z1F8; A5YWM4; Q17065;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 25-MAY-2022, entry version 65.
DE RecName: Full=Arylphorin;
DE Flags: Precursor;
OS Antheraea pernyi (Chinese oak silk moth) (Bombyx pernyi).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Saturniidae; Saturniinae; Saturniini; Antheraea.
OX NCBI_TaxID=7119;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND GLYCOSYLATION AT ASN-212 AND ASN-360.
RC TISSUE=Fat body;
RA Cho O., Lee S.M., Park N.S., Jin B.R., Kim S.;
RT "Arylphorin of Antheraea pernyi.";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Zhang X.M., Liu N., Wei A.H., Cui S.S., Jiang S., Yan W.Q.;
RT "The research of Antheraea pernyi arylphorin precursor promoter.";
RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 251-371.
RC STRAIN=Hotaka; TISSUE=Posterior silk gland;
RX PubMed=8845960; DOI=10.1006/mpev.1995.1021;
RA Shimada T., Kurimoto Y., Kobayashi M.;
RT "Phylogenetic relationship of silkmoths inferred from sequence data of the
RT arylphorin gene.";
RL Mol. Phylogenet. Evol. 4:223-234(1995).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.43 ANGSTROMS) OF 24-697, SUBUNIT, GLYCOSYLATION AT
RP ASN-212 AND ASN-360, AND INTERCHAIN DISULFIDE BONDS.
RX PubMed=19358695; DOI=10.1042/bj20082170;
RA Ryu K.S., Lee J.O., Kwon T.H., Choi H.H., Park H.S., Hwang S.K., Lee Z.W.,
RA Lee K.B., Han Y.H., Choi Y.S., Jeon Y.H., Cheong C., Kim S.;
RT "The presence of monoglucosylated N196-glycan is important for the
RT structural stability of storage protein, arylphorin.";
RL Biochem. J. 421:87-96(2009).
CC -!- FUNCTION: Arylphorin is a larval storage protein (LSP) which may serve
CC as a storage protein used primarily as a source of aromatic amino acids
CC for protein synthesis during metamorphosis. It is a constituent of the
CC sclerotizing system of the cuticle, and serves as a carrier for
CC ecdysteroid hormone (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homohexamer of two stacked trimers; disulfide-linked.
CC {ECO:0000269|PubMed:19358695}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000250}.
CC -!- PTM: Glycosylation at Asn-360 is required for proper folding.
CC {ECO:0000269|PubMed:19358695, ECO:0000269|Ref.1}.
CC -!- SIMILARITY: Belongs to the hemocyanin family. {ECO:0000305}.
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DR EMBL; AY278025; AAP34685.1; -; mRNA.
DR EMBL; EF597564; ABQ96634.1; -; Genomic_DNA.
DR EMBL; D44483; BAA07926.1; -; Genomic_DNA.
DR PDB; 3GWJ; X-ray; 2.43 A; A/B/C/D/E/F=24-697.
DR PDBsum; 3GWJ; -.
DR AlphaFoldDB; Q7Z1F8; -.
DR SMR; Q7Z1F8; -.
DR GlyConnect; 60; 10 N-Linked glycans.
DR iPTMnet; Q7Z1F8; -.
DR EvolutionaryTrace; Q7Z1F8; -.
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; PS00209; HEMOCYANIN_1; 1.
DR PROSITE; PS00210; HEMOCYANIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Glycoprotein; Secreted; Signal;
KW Storage protein.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..704
FT /note="Arylphorin"
FT /id="PRO_0000013328"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19358695, ECO:0000269|Ref.1"
FT CARBOHYD 360
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19358695, ECO:0000269|Ref.1"
FT DISULFID 89
FT /note="Interchain (with C-665)"
FT DISULFID 665
FT /note="Interchain (with C-89)"
FT CONFLICT 3
FT /note="I -> T (in Ref. 2; ABQ96634)"
FT /evidence="ECO:0000305"
FT CONFLICT 82
FT /note="D -> E (in Ref. 2; ABQ96634)"
FT /evidence="ECO:0000305"
FT CONFLICT 548
FT /note="W -> R (in Ref. 2; ABQ96634)"
FT /evidence="ECO:0000305"
FT CONFLICT 555
FT /note="D -> E (in Ref. 2; ABQ96634)"
FT /evidence="ECO:0000305"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:3GWJ"
FT HELIX 33..44
FT /evidence="ECO:0007829|PDB:3GWJ"
FT HELIX 57..64
FT /evidence="ECO:0007829|PDB:3GWJ"
FT HELIX 68..73
FT /evidence="ECO:0007829|PDB:3GWJ"
FT HELIX 77..87
FT /evidence="ECO:0007829|PDB:3GWJ"
FT HELIX 103..117
FT /evidence="ECO:0007829|PDB:3GWJ"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:3GWJ"
FT HELIX 122..135
FT /evidence="ECO:0007829|PDB:3GWJ"
FT HELIX 138..151
FT /evidence="ECO:0007829|PDB:3GWJ"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:3GWJ"
FT HELIX 163..166
FT /evidence="ECO:0007829|PDB:3GWJ"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:3GWJ"
FT HELIX 174..186
FT /evidence="ECO:0007829|PDB:3GWJ"
FT HELIX 192..195
FT /evidence="ECO:0007829|PDB:3GWJ"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:3GWJ"
FT STRAND 200..203
FT /evidence="ECO:0007829|PDB:3GWJ"
FT STRAND 206..210
FT /evidence="ECO:0007829|PDB:3GWJ"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:3GWJ"
FT HELIX 222..226
FT /evidence="ECO:0007829|PDB:3GWJ"
FT HELIX 227..230
FT /evidence="ECO:0007829|PDB:3GWJ"
FT HELIX 233..245
FT /evidence="ECO:0007829|PDB:3GWJ"
FT HELIX 253..256
FT /evidence="ECO:0007829|PDB:3GWJ"
FT HELIX 257..260
FT /evidence="ECO:0007829|PDB:3GWJ"
FT HELIX 262..283
FT /evidence="ECO:0007829|PDB:3GWJ"
FT STRAND 298..300
FT /evidence="ECO:0007829|PDB:3GWJ"
FT STRAND 309..312
FT /evidence="ECO:0007829|PDB:3GWJ"
FT HELIX 325..327
FT /evidence="ECO:0007829|PDB:3GWJ"
FT HELIX 328..347
FT /evidence="ECO:0007829|PDB:3GWJ"
FT HELIX 364..373
FT /evidence="ECO:0007829|PDB:3GWJ"
FT HELIX 376..378
FT /evidence="ECO:0007829|PDB:3GWJ"
FT STRAND 381..383
FT /evidence="ECO:0007829|PDB:3GWJ"
FT HELIX 391..400
FT /evidence="ECO:0007829|PDB:3GWJ"
FT HELIX 415..417
FT /evidence="ECO:0007829|PDB:3GWJ"
FT TURN 419..421
FT /evidence="ECO:0007829|PDB:3GWJ"
FT HELIX 422..424
FT /evidence="ECO:0007829|PDB:3GWJ"
FT HELIX 426..442
FT /evidence="ECO:0007829|PDB:3GWJ"
FT HELIX 443..445
FT /evidence="ECO:0007829|PDB:3GWJ"
FT HELIX 451..454
FT /evidence="ECO:0007829|PDB:3GWJ"
FT STRAND 459..466
FT /evidence="ECO:0007829|PDB:3GWJ"
FT STRAND 469..479
FT /evidence="ECO:0007829|PDB:3GWJ"
FT HELIX 481..483
FT /evidence="ECO:0007829|PDB:3GWJ"
FT HELIX 490..492
FT /evidence="ECO:0007829|PDB:3GWJ"
FT STRAND 499..508
FT /evidence="ECO:0007829|PDB:3GWJ"
FT STRAND 512..521
FT /evidence="ECO:0007829|PDB:3GWJ"
FT STRAND 523..535
FT /evidence="ECO:0007829|PDB:3GWJ"
FT HELIX 544..547
FT /evidence="ECO:0007829|PDB:3GWJ"
FT HELIX 548..550
FT /evidence="ECO:0007829|PDB:3GWJ"
FT STRAND 552..561
FT /evidence="ECO:0007829|PDB:3GWJ"
FT STRAND 563..571
FT /evidence="ECO:0007829|PDB:3GWJ"
FT HELIX 572..574
FT /evidence="ECO:0007829|PDB:3GWJ"
FT HELIX 585..592
FT /evidence="ECO:0007829|PDB:3GWJ"
FT TURN 593..595
FT /evidence="ECO:0007829|PDB:3GWJ"
FT STRAND 596..598
FT /evidence="ECO:0007829|PDB:3GWJ"
FT HELIX 599..603
FT /evidence="ECO:0007829|PDB:3GWJ"
FT STRAND 607..609
FT /evidence="ECO:0007829|PDB:3GWJ"
FT HELIX 610..612
FT /evidence="ECO:0007829|PDB:3GWJ"
FT STRAND 622..632
FT /evidence="ECO:0007829|PDB:3GWJ"
FT TURN 641..643
FT /evidence="ECO:0007829|PDB:3GWJ"
FT STRAND 649..651
FT /evidence="ECO:0007829|PDB:3GWJ"
FT TURN 653..656
FT /evidence="ECO:0007829|PDB:3GWJ"
FT STRAND 657..659
FT /evidence="ECO:0007829|PDB:3GWJ"
FT STRAND 671..680
FT /evidence="ECO:0007829|PDB:3GWJ"
FT HELIX 686..690
FT /evidence="ECO:0007829|PDB:3GWJ"
FT HELIX 692..695
FT /evidence="ECO:0007829|PDB:3GWJ"
SQ SEQUENCE 704 AA; 83574 MW; A1181D49D8391E7C CRC64;
MKIVLVLAGL IALVQSSVVH PPPHVLKTKD VDTVFVERQK KVLSLFQDVD QLNTNDEYYK
IGKDYDIEAN IDNYTNKKAV EDFLKMYRCG FLPKYNEFSV FHDKLRDEAI ALFHLFYYAK
DFDTFYKSAA FARVHLNQGQ FLYAYYIAII QRKDTYGIVL PAPYEIYPEL FVNIDTTYKM
FRTKMQNGLI NPEAAVEYGI VKEDNHYVYY SNYSNAITYY NEEQRLAYFT EDIGLNAYYF
FFHIHLPFWW TAEKYGNLKE RRGEMYHYFY DQLLTRYYFE RLTNGLGTIP EFSWYSPVKT
GHYPLLTSYY TPFSQRPNFY NVHSEENYEK IRFLDAYENY FVQALQKGVF EGFGQTIYLN
DSKANSFVGN YWQDNADLYG EEVTKDYQRS YEIVARQVLG AAPKPFDKYT FMPSALDFYQ
TSLRDPTFYQ LYNRIIGYFN QFKQYLEPHS QEKLHFVGVK VNNVVVDKLV TFFEYYDFDA
TNTVFLTEEE LKTKYPHNLK VRQPRLNHQP FNINIDIKAD VATDAVVKIF MGPKYNENGF
PITLENDWMK FFEMDWFTHK ITPGQNTIVR NSNEFVIFKE DSLPSTELYK LLEKGKVPFD
MSEDFGYLPK RLMLPRGTKG GFPFQFVVFV YPFESTTKNL TPYEKFMIDN KPLGYPFDRP
VDTSCFKQPN IFFRDVSVYH EGEYHAYEYN VPAYFSHTNK VPKE
