ID   ARYA_MANSE              Reviewed;         702 AA.
AC   P14296;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=Arylphorin subunit alpha;
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; M28394; AAA29302.1; -; Genomic_DNA.
DR   EMBL; M28396; AAA29303.1; -; mRNA.
DR   PIR; A34434; A34434.
DR   AlphaFoldDB; P14296; -.
DR   SMR; P14296; -.
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..702
FT                   /note="Arylphorin subunit alpha"
FT                   /id="PRO_0000013329"
FT   CARBOHYD        75
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        214
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   702 AA;  83866 MW;  0B0E863DE6265D0B CRC64;
     MKTVVILAGL VALALSSAVP PPKYQHHYKT SPVDAIFVEK QKKVFSLFKN VNQLDYEAEY
     YKIGKDYDVE ANIDNYSNKK VVEDFLLLYR TGFMPKGFEF SIFYERMREE AIALFELFYY
     AKDFETFYKT ASFARVHVNE GMFLYAYYIA VIQRMDTNGL VLPAPYEVYP QYFTNMEVLF
     KVDRIKMQDG FLNKDLAAYY GMYHENDNYV FYANYSNSLS YPNEEERIAY FYEDIGLNSY
     YYYFHMHLPF WWNSEKYGPF KERRGEIYYY FYQQLIARYY LERLTNGLGE IPEFSWYSPV
     KTGYYPMLYG SYYPFAQRPN YYDIHNDKNY EQIRFLDMFE MTFLQYLQKG HFKAFDKEIN
     FHDVKAVNFV GNYWQANADL YNEEVTKLYQ RSYEINARHV LGAAPKPFNK YSFIPSALDF
     YQTSLRDPVF YQLYDRIINY INEFKQYLQP YNQNDLHFVG VKISDVKVDK LATYFEYYDF
     DVSNSVFVSK KDIKNFPYGY KVRQPRLNHK PFSVSIGVKS DVAVDAVFKI FLGPKYDSNG
     FPIPLAKNWN KFYELDWFVH KVMPGQNHIV RQSSDFLFFK EDSLPMSEIY KLLDEGKIPS
     DMSNSSDTLP QRLMLPRGTK DGYPFQLFVF VYPYQAVPKE MEPFKSIVPD SKPFGYPFDR
     PVHPEYFKQP NMHFEDVHVY HEGEQFPYKF NVPFYVPQKV EV