ARY1_CALVI
ID ARY1_CALVI Reviewed; 759 AA.
AC P28513; Q23815;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=Arylphorin subunit A4;
DE Flags: Precursor;
OS Calliphora vicina (Blue blowfly) (Calliphora erythrocephala).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Oestroidea;
OC Calliphoridae; Calliphorinae; Calliphora.
OX NCBI_TaxID=7373;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fat body;
RX PubMed=1711849; DOI=10.1016/0006-291x(91)90632-h;
RA Naumann U., Scheller K.;
RT "Complete cDNA and gene sequence of the developmentally regulated
RT arylphorin of Calliphora vicina and its homology to insect hemolymph
RT proteins and arthropod hemocyanins.";
RL Biochem. Biophys. Res. Commun. 177:963-972(1991).
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: Heterohexamer.
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; M76480; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; X59391; CAA42034.1; -; mRNA.
DR PIR; JQ1045; JQ1045.
DR AlphaFoldDB; P28513; -.
DR SMR; P28513; -.
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; 2.
DR Pfam; PF03722; Hemocyanin_N; 2.
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 Secreted; Signal; Storage protein.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..759
FT /note="Arylphorin subunit A4"
FT /id="PRO_0000013331"
FT CONFLICT 231
FT /note="N -> D (in Ref. 1; CAA42034)"
FT /evidence="ECO:0000305"
FT CONFLICT 351
FT /note="N -> H (in Ref. 1; CAA42034)"
FT /evidence="ECO:0000305"
FT CONFLICT 607
FT /note="D -> E (in Ref. 1; CAA42034)"
FT /evidence="ECO:0000305"
FT CONFLICT 683
FT /note="G -> E (in Ref. 1; CAA42034)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 759 AA; 92342 MW; 3D222108A38B4BBD CRC64;
MKIAIVLLAI IALVAASSIS KHEVKIADKE FLAKQKFLFE IVYRVEDPLM FEEWIKMGKT
FTFDKSGYTH FDMYMEKFYE AYKYGAILPK GEFFYYAKNW ETFQRNVAFA RMHFNEGMFV
YALTLAVIHR DDFQGLILPS IHEIFPQYFF NSKFVYEAEK FDYDVWSKYI MYEKEYKDIL
YKDYSTFYKN HDNHHYYYFT KDFKTYQWWK MMGLGEHWYS EDRFMLRDNM NKYNKDSKYL
EIFEGTKMFF MPVDYTRDIE FFNKESVLSY FTEDVGLNTY WYYLNMDYAF ILDGKTFGLN
KDRRGEYWLY NVRQLLSRYY MERLTHGYGE IPHFSFLNTI EHGYDSQLVY NNGVGFSYRK
NYYEVESYGK FSYYYKVMDF FNRLDEIITK GVYVTYEGKT IDLRKPESIE YIGSIMQGNV
DTFDNYFFKY RYMFAHMYFG DVNTHDFEVF PHIFLNYETM MRDPMFYMFY KKIASVYFQF
FNYVKPYTHE ELLFPGVTIK DVKVSELVTY FDLVDFDVTN LMNDEMTFVD GQFVWDKTLL
ARQMRLNHKP FDFDFVIESD KSHKVVIRTF LGPKYDEFGR VITLTENRQN FMEIDSFIYT
LKSGVNDFKR LSKDFYWTVE DRTTYNELYK YVMLALQGKY DFPLDISEPH CGFPDRLVLP
HGWYKGMPMQ FFFYIAPYTA SYGPFSTYDS TYACGIGSGV RHIDEMPFGY PFDREIDEYE
FFVPNMYFKD VKIYHQDTFD KYYGKKYENF GHFDYSYYH