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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
 
 
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