HCYA_PANIN
ID HCYA_PANIN Reviewed; 657 AA.
AC P04254;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 2.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Hemocyanin A chain;
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.
RA Bak H.J., Neuteboom B., Jekel P.A., Soeter N.M., Vereijken J.M.,
RA Beintema J.J.;
RT "Structure of arthropod hemocyanin.";
RL FEBS Lett. 204:141-144(1986).
RN [2]
RP PROTEIN SEQUENCE.
RX PubMed=3480218; DOI=10.1111/j.1432-1033.1987.tb13616.x;
RA Bak H.J., Beintema J.J.;
RT "Panulirus interruptus hemocyanin. The elucidation of the complete amino
RT acid sequence of subunit a.";
RL Eur. J. Biochem. 169:333-348(1987).
RN [3]
RP PROTEIN SEQUENCE OF 1-158.
RX PubMed=3319611; DOI=10.1111/j.1432-1033.1987.tb13615.x;
RA Soeter N.M., Jekel P.A., Beintema J.J., Volbeda A., Hol W.G.J.;
RT "Primary and tertiary structures of the first domain of Panulirus
RT interruptus hemocyanin and comparison of arthropod hemocyanins.";
RL Eur. J. Biochem. 169:323-332(1987).
RN [4]
RP PROTEIN SEQUENCE OF 160-230.
RA Vereijken J.M., de Vlieg J., Beintema J.J.;
RT "Panulirus interruptus hemocyanin. The amino-acid sequence of the region
RT containing one copper-binding site and the sites susceptible to limited
RT proteolysis.";
RL Biochim. Biophys. Acta 788:298-305(1984).
RN [5]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=3208765; DOI=10.1111/j.1432-1033.1988.tb14464.x;
RA Jekel P.A., Bak H.J., Soeter N.M., Verejken J.M., Beintema J.J.;
RT "Panulirus interruptus hemocyanin. The amino acid sequence of subunit b and
RT anomalous behaviour of subunits a and b on polyacrylamide gel
RT electrophoresis in the presence of SDS.";
RL Eur. J. Biochem. 178:403-412(1988).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS), FUNCTION, SUBUNIT, AND DISULFIDE
RP BONDS.
RA Gaykema W.P.J., Hol W.G.J., Vereijken J.M., Soeter N.M., Bak H.J.,
RA Beintema J.J.;
RT "3.2-A structure of the copper-containing, oxygen-carrying protein
RT Panulirus interruptus haemocyanin.";
RL Nature 309:23-29(1984).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS), FUNCTION, SUBUNIT, COPPER-BINDING
RP SITES, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-167.
RX PubMed=2585484; DOI=10.1016/0022-2836(89)90276-3;
RA Volbeda A., Hol W.G.J.;
RT "Crystal structure of hexameric haemocyanin from Panulirus interruptus
RT refined at 3.2-A resolution.";
RL J. Mol. Biol. 209:249-279(1989).
CC -!- FUNCTION: Hemocyanins are copper-containing oxygen carriers occurring
CC freely dissolved in the hemolymph of many mollusks and arthropods.
CC {ECO:0000269|PubMed:2585484, ECO:0000269|Ref.6}.
CC -!- SUBUNIT: Hexamer of a number of different chains, of which A, B, and C
CC have been identified. {ECO:0000269|PubMed:2585484, ECO:0000269|Ref.6}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC {ECO:0000269|PubMed:3208765}.
CC -!- TISSUE SPECIFICITY: Hemolymph. {ECO:0000269|PubMed:3208765}.
CC -!- MISCELLANEOUS: The A chain contains two copper-binding sites (Ref.6,
CC PubMed:2585484). Three histidine residues are ligands to each copper
CC ion (Ref.6, PubMed:2585484). {ECO:0000269|PubMed:2585484,
CC ECO:0000269|Ref.6}.
CC -!- SIMILARITY: Belongs to the tyrosinase family. Hemocyanin subfamily.
CC {ECO:0000305}.
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DR PIR; A24183; BHLOA.
DR PDB; 1HC1; X-ray; 3.20 A; A/B/C/D/E/F=1-657.
DR PDB; 1HCY; X-ray; 3.20 A; A/B/C/D/E/F=1-657.
DR PDBsum; 1HC1; -.
DR PDBsum; 1HCY; -.
DR AlphaFoldDB; P04254; -.
DR SMR; P04254; -.
DR EvolutionaryTrace; P04254; -.
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 3D-structure; Copper; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Metal-binding; Oxygen transport; Secreted; Transport.
FT CHAIN 1..657
FT /note="Hemocyanin A chain"
FT /id="PRO_0000204291"
FT REGION 594..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 194
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000269|PubMed:2585484,
FT ECO:0007744|PDB:1HC1, ECO:0007744|PDB:1HCY"
FT BINDING 198
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000269|PubMed:2585484,
FT ECO:0007744|PDB:1HC1, ECO:0007744|PDB:1HCY"
FT BINDING 224
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000269|PubMed:2585484,
FT ECO:0007744|PDB:1HC1, ECO:0007744|PDB:1HCY"
FT BINDING 344
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000269|PubMed:2585484,
FT ECO:0007744|PDB:1HC1, ECO:0007744|PDB:1HCY"
FT BINDING 348
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000269|PubMed:2585484,
FT ECO:0007744|PDB:1HC1, ECO:0007744|PDB:1HCY"
FT BINDING 384
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000269|PubMed:2585484,
FT ECO:0007744|PDB:1HC1, ECO:0007744|PDB:1HCY"
FT CARBOHYD 167
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:2585484,
FT ECO:0007744|PDB:1HCY"
FT DISULFID 93..98
FT /evidence="ECO:0000269|PubMed:2585484, ECO:0000269|Ref.6,
FT ECO:0007744|PDB:1HC1, ECO:0007744|PDB:1HCY"
FT DISULFID 483..502
FT /evidence="ECO:0000269|PubMed:2585484, ECO:0000269|Ref.6,
FT ECO:0007744|PDB:1HC1, ECO:0007744|PDB:1HCY"
FT DISULFID 562..609
FT /evidence="ECO:0000269|PubMed:2585484, ECO:0000269|Ref.6,
FT ECO:0007744|PDB:1HC1, ECO:0007744|PDB:1HCY"
FT HELIX 8..17
FT /evidence="ECO:0007829|PDB:1HC1"
FT TURN 18..22
FT /evidence="ECO:0007829|PDB:1HC1"
FT HELIX 28..36
FT /evidence="ECO:0007829|PDB:1HC1"
FT STRAND 45..50
FT /evidence="ECO:0007829|PDB:1HC1"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:1HC1"
FT HELIX 56..61
FT /evidence="ECO:0007829|PDB:1HC1"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:1HC1"
FT HELIX 77..90
FT /evidence="ECO:0007829|PDB:1HC1"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:1HC1"
FT HELIX 96..105
FT /evidence="ECO:0007829|PDB:1HC1"
FT TURN 106..109
FT /evidence="ECO:0007829|PDB:1HC1"
FT HELIX 112..125
FT /evidence="ECO:0007829|PDB:1HC1"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:1HCY"
FT HELIX 137..140
FT /evidence="ECO:0007829|PDB:1HC1"
FT TURN 142..145
FT /evidence="ECO:0007829|PDB:1HC1"
FT HELIX 148..160
FT /evidence="ECO:0007829|PDB:1HC1"
FT TURN 174..176
FT /evidence="ECO:0007829|PDB:1HCY"
FT HELIX 182..185
FT /evidence="ECO:0007829|PDB:1HC1"
FT HELIX 188..200
FT /evidence="ECO:0007829|PDB:1HC1"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:1HC1"
FT HELIX 218..236
FT /evidence="ECO:0007829|PDB:1HC1"
FT TURN 237..239
FT /evidence="ECO:0007829|PDB:1HC1"
FT STRAND 250..252
FT /evidence="ECO:0007829|PDB:1HCY"
FT STRAND 263..265
FT /evidence="ECO:0007829|PDB:1HC1"
FT STRAND 273..275
FT /evidence="ECO:0007829|PDB:1HC1"
FT TURN 281..283
FT /evidence="ECO:0007829|PDB:1HC1"
FT HELIX 286..302
FT /evidence="ECO:0007829|PDB:1HC1"
FT STRAND 303..306
FT /evidence="ECO:0007829|PDB:1HC1"
FT STRAND 308..310
FT /evidence="ECO:0007829|PDB:1HC1"
FT STRAND 312..314
FT /evidence="ECO:0007829|PDB:1HC1"
FT HELIX 320..328
FT /evidence="ECO:0007829|PDB:1HC1"
FT TURN 337..339
FT /evidence="ECO:0007829|PDB:1HC1"
FT HELIX 343..352
FT /evidence="ECO:0007829|PDB:1HC1"
FT HELIX 353..355
FT /evidence="ECO:0007829|PDB:1HC1"
FT HELIX 367..369
FT /evidence="ECO:0007829|PDB:1HC1"
FT TURN 371..373
FT /evidence="ECO:0007829|PDB:1HC1"
FT HELIX 374..376
FT /evidence="ECO:0007829|PDB:1HCY"
FT HELIX 379..395
FT /evidence="ECO:0007829|PDB:1HC1"
FT HELIX 403..406
FT /evidence="ECO:0007829|PDB:1HC1"
FT STRAND 409..420
FT /evidence="ECO:0007829|PDB:1HC1"
FT STRAND 423..426
FT /evidence="ECO:0007829|PDB:1HC1"
FT STRAND 429..432
FT /evidence="ECO:0007829|PDB:1HC1"
FT HELIX 433..436
FT /evidence="ECO:0007829|PDB:1HC1"
FT STRAND 441..443
FT /evidence="ECO:0007829|PDB:1HCY"
FT STRAND 449..452
FT /evidence="ECO:0007829|PDB:1HC1"
FT STRAND 455..457
FT /evidence="ECO:0007829|PDB:1HC1"
FT STRAND 461..468
FT /evidence="ECO:0007829|PDB:1HC1"
FT STRAND 470..472
FT /evidence="ECO:0007829|PDB:1HC1"
FT STRAND 475..483
FT /evidence="ECO:0007829|PDB:1HC1"
FT STRAND 488..490
FT /evidence="ECO:0007829|PDB:1HC1"
FT TURN 497..501
FT /evidence="ECO:0007829|PDB:1HC1"
FT STRAND 503..511
FT /evidence="ECO:0007829|PDB:1HC1"
FT STRAND 517..522
FT /evidence="ECO:0007829|PDB:1HC1"
FT TURN 523..525
FT /evidence="ECO:0007829|PDB:1HC1"
FT HELIX 536..543
FT /evidence="ECO:0007829|PDB:1HC1"
FT STRAND 546..548
FT /evidence="ECO:0007829|PDB:1HC1"
FT STRAND 558..560
FT /evidence="ECO:0007829|PDB:1HC1"
FT STRAND 563..565
FT /evidence="ECO:0007829|PDB:1HC1"
FT HELIX 566..568
FT /evidence="ECO:0007829|PDB:1HC1"
FT STRAND 578..587
FT /evidence="ECO:0007829|PDB:1HC1"
FT HELIX 589..592
FT /evidence="ECO:0007829|PDB:1HC1"
FT TURN 622..627
FT /evidence="ECO:0007829|PDB:1HC1"
FT TURN 633..635
FT /evidence="ECO:0007829|PDB:1HC1"
FT HELIX 636..638
FT /evidence="ECO:0007829|PDB:1HC1"
FT STRAND 642..651
FT /evidence="ECO:0007829|PDB:1HC1"
SQ SEQUENCE 657 AA; 75696 MW; FB5520EDD2667D85 CRC64;
DALGTGNAQK QQDINHLLDK IYEPTKYPDL KEIAENFNPL GDTSIYNDHG AAVETLMKEL
NDHRLLEQRH WYSLFNTRQR KEALMLFAVL NQCKEWYCFR SNAAYFRERM NEGEFVYALY
VSVIHSKLGD GIVLPPLYQI TPHMFTNSEV IDKAYSAKMT QKQGTFNVSF TGTKKNREQR
VAYFGEDIGM NIHHVTWHMD FPFWWEDSYG YHLDRKGELF FWVHHQLTAR FDFERLSNWL
DPVDELHWDR IIREGFAPLT SYKYGGEFPV RPDNIHFEDV DGVAHVHDLE ITESRIHEAI
DHGYITDSDG HTIDIRQPKG IELLGDIIES SKYSSNVQYY GSLHNTAHVM LGRQGDPHGK
FNLPPGVMEH FETATRDPSF FRLHKYMDNI FKKHTDSFPP YTHDNLEFSG MVVNGVAIDG
ELITFFDEFQ YSLINAVDSG ENIEDVEINA RVHRLNHKEF TYKITMSNNN DGERLATFRI
FLCPIEDNNG ITLTLDEARW FCIELDKFFQ KVPKGPETIE RSSKDSSVTV PDMPSFQSLK
EQADNAVNGG HDLDLSAYER SCGIPDRMLL PKSKPEGMEF NLYVAVTDGD KDTEGHNGGH
DYGGTHAQCG VHGEAYPDNR PLGYPLERRI PDERVIDGVS NIKHVVVKIV HHLEHHD
