HCYC_PANIN
ID HCYC_PANIN Reviewed; 661 AA.
AC P80096;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Hemocyanin C chain {ECO:0000303|PubMed:1587275};
OS Panulirus interruptus (California spiny lobster) (Palinurus interruptus).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Achelata;
OC Palinuroidea; Palinuridae; Panulirus.
OX NCBI_TaxID=6735;
RN [1]
RP PROTEIN SEQUENCE, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Hemolymph;
RX PubMed=1587275; DOI=10.1111/j.1432-1033.1992.tb16922.x;
RA Neuteboom B., Jekel P.A., Beintema J.J.;
RT "Primary structure of hemocyanin subunit c from Panulirus interruptus.";
RL Eur. J. Biochem. 206:243-249(1992).
RN [2]
RP PARTIAL PROTEIN SEQUENCE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DISULFIDE BOND.
RC TISSUE=Hemolymph;
RA Neuteboom B., Jekel P.A., Hofstra R.M.W., Beintema J.J.;
RT "Sulfhydryl groups and disulfide bridges in subunit c of Panulirus
RT interruptus hemocyanin.";
RL Biochim. Biophys. Acta 998:126-130(1989).
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, of which A, B, and C
CC have been identified. {ECO:0000250|UniProtKB:P04254}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC {ECO:0000269|PubMed:1587275, ECO:0000269|Ref.2}.
CC -!- TISSUE SPECIFICITY: Hemolymph. {ECO:0000269|PubMed:1587275,
CC ECO:0000269|Ref.2}.
CC -!- SIMILARITY: Belongs to the tyrosinase family. Hemocyanin subfamily.
CC {ECO:0000305}.
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DR PIR; S21221; S21221.
DR AlphaFoldDB; P80096; -.
DR SMR; P80096; -.
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 C chain"
FT /id="PRO_0000204293"
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:0000269|Ref.2"
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
