ARYB_MANSE
ID ARYB_MANSE Reviewed; 703 AA.
AC P14297;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Arylphorin subunit beta;
DE Flags: Precursor;
OS Manduca sexta (Tobacco hawkmoth) (Tobacco hornworm).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Sphingidae; Sphinginae; Sphingini; Manduca.
OX NCBI_TaxID=7130;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC TISSUE=Larval fat body;
RX PubMed=2808410; DOI=10.1016/s0021-9258(19)47265-7;
RA Willott E., Wang X.-Y., Wells M.A.;
RT "cDNA and gene sequence of Manduca sexta arylphorin, an aromatic amino
RT acid-rich larval serum protein. Homology to arthropod hemocyanins.";
RL J. Biol. Chem. 264:19052-19059(1989).
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.
CC -!- SUBUNIT: Arylphorin is a hexamer of subunits alpha and beta.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC -!- TISSUE SPECIFICITY: Fat body.
CC -!- SIMILARITY: Belongs to the hemocyanin family. {ECO:0000305}.
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DR EMBL; M28395; AAA29304.1; -; Genomic_DNA.
DR EMBL; M28397; AAA29305.1; -; mRNA.
DR PIR; B34434; B34434.
DR AlphaFoldDB; P14297; -.
DR SMR; P14297; -.
DR PRIDE; P14297; -.
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 2: Evidence at transcript level;
KW Glycoprotein; Secreted; Signal; Storage protein.
FT SIGNAL 1..16
FT CHAIN 17..703
FT /note="Arylphorin subunit beta"
FT /id="PRO_0000013330"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 703 AA; 83849 MW; 24B7DBBB60D2E3FA CRC64;
MKTVIILAGL VALALGSEVP VKHSFKVKDV DAAFVERQKK VLDLFQDVDQ VNPNDEYYKI
GKEYNIEANI DNYSNKKAVE EFLQLYRTGF LPKYYEFSPF YDRLRDEAIG VFHLFYYAKD
FDTFYKSAAW ARVYLNEGQF LYAYYIAVIQ RKDTQGFVVP APYEVYPQFF ANLNTMLKVY
RTKMQDGVVS ADLAAQHGIV KEKNYYVYYA NYSNSLVYNN EEQRLSYFTE DIGLNSYYYY
FHSHLPFWWN SERYGALKSR RGEIYYYFYQ QLMARYYFER LSNGLGDIPE FSWYSPVKSG
YYPLMSSYYY PFAQRPNYWN VHSEENYEKV RFLDTYEMSF LQFLQNGHFK AFDQKIDFHD
FKAINFVGNY WQDNADLYGE EVTKDYQRSY EIIARQVLGA APKPFDKYTF MPSALDFYQT
SLRDPMFYQL YNRILKYIYE YKQYLQPYSS EKLAFKGVKV VDVVVDKLVT FFEYYDFDAS
NSVFWSKEEV KSSYPHDFKI RQPRLNHKPF SVSIDIKSEA AVDAVVKIFM APKYDDNGFP
LKLENNWNKF FELDWFTYKF VAGDNKIVRN SNDFLIFKDD SVPMTELYKL LEQNKVPHDM
SEDYGYLPKR LMLPRGTEGG FPFQFFVFVY PFNADSKDLA PFEAFIQDNK PLGYPFDRPV
VDAYFKQHNM FFKDVFVYHD GEYFPYKFNV PSHVMHSNVV PKH