ID   HCY_SCYOL               Reviewed;         661 AA.
AC   C0HLU7;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   29-SEP-2021, sequence version 1.
DT   03-AUG-2022, entry version 4.
DE   RecName: Full=Hemocyanin subunit {ECO:0000303|Ref.1};
OS   Scylla olivacea (Orange mud crab) (Cancer olivacea).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC   Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Brachyura;
OC   Eubrachyura; Portunoidea; Portunidae; Scylla.
OX   NCBI_TaxID=85551 {ECO:0000303|Ref.1};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR
RP   LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Hemolymph {ECO:0000269|Ref.1};
RA   Prasanthi C., Ramesh B.K.;
RT   "Characterization and molecular interactions of hemolymph proteins from two
RT   mud crab species Scylla serrata (Forskal, 1775) and Scylla olivacea
RT   (Herbst, 1796) from Visakhapatnam coast, Andhra Pradesh, India.";
RL   Submitted (DEC-2020) to UniProtKB.
CC   -!- FUNCTION: Hemocyanins are copper-containing oxygen carriers occurring
CC       freely dissolved in the hemolymph of many mollusks and arthropods.
CC       {ECO:0000250|UniProtKB:P04254}.
CC   -!- SUBUNIT: Hexamer of a number of different chains.
CC       {ECO:0000250|UniProtKB:P04254}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC       {ECO:0000269|Ref.1}.
CC   -!- TISSUE SPECIFICITY: Hemolymph. {ECO:0000269|Ref.1}.
CC   -!- SIMILARITY: Belongs to the tyrosinase family. Hemocyanin subfamily.
CC       {ECO:0000305}.
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DR   SMR; C0HLU7; -.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0005344; F:oxygen carrier 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   InterPro; IPR002227; Tyrosinase_Cu-bd.
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.
DR   PROSITE; PS00498; TYROSINASE_2; 1.
PE   1: Evidence at protein level;
KW   Copper; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Metal-binding; Oxygen transport; Secreted; Transport.
FT   CHAIN           1..661
FT                   /note="Hemocyanin subunit"
FT                   /id="PRO_0000453528"
FT   BINDING         200
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250|UniProtKB:P04254"
FT   BINDING         204
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250|UniProtKB:P04254"
FT   BINDING         230
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250|UniProtKB:P04254"
FT   BINDING         350
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250|UniProtKB:P04254"
FT   BINDING         354
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250|UniProtKB:P04254"
FT   BINDING         390
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250|UniProtKB:P04254"
FT   CARBOHYD        476
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        3..557
FT                   /evidence="ECO:0000250|UniProtKB:P80096"
SQ   SEQUENCE   661 AA;  75874 MW;  F31F4338168B4069 CRC64;
     ADCQAGDSAD KLLAQKQHDV NYLVYKLYGD IRDDHLKELG ETFNPQGDLL LYHDNGASVN
     TLMADFKDGR LLQKKHWFSL FNTRQREEAL MMHRVLMNCK NWHAFVSNAA YFRTNMNEGE
     YLYALYVSLI HSGLGEGVVL PPLYEVTPHM FTNSEVIHEA YKAQMTNTPS KFESHFTGSK
     KNPEQHVAYF GEDVGMNTHH VLWHMEFPFW WEDSSGRHLD RKGESFFWVH HQLTVRYDAE
     RLSNHLDPVE ELSWNKAIDE GFAPHTAYKY GGYFPSRPDN VHFSDVDGVA RVRDMSMTED
     RIRDAIAHGY IDALDGSHID IMNSHGIEFL GDIIESSGYS ANPGFYGSLH NTAHIMLGRQ
     GDPTGKFDLP PGVLEHFETS TRDPSFFRLH KYMDNIFREH KDSLTPYTRD ELEFNGVSID
     SIAIEGTLET FFENFEYSLL NAVDDTVDIA DVEILTYIER LNHKKFSFLI LVTNNNNTEV
     LATVRIFAWP LRDNNGIEYS FNEGRWRALE LDRFWVKVKH GHHQITRQST ESSVTVPDVP
     SLQTLIDRAD AAISSGCALH LEDYESALGL PNRFLLPKGQ AQGMEFNLVV AVTDGRTDAA
     LDDLHENTKF IHYGYDRQYP DKRPHGYPLD RRVDDERIFE ALPNFKQRTV KLYSHEGVDG
     G