ID   HCYB_PANIN              Reviewed;         657 AA.
AC   P10787;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Hemocyanin B 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, 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   [2]
RP   X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS), FUNCTION, AND SUBUNIT.
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   [3]
RP   X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS), FUNCTION, SUBUNIT, COPPER-BINDING
RP   SITES, AND DISULFIDE BOND.
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.2}.
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.2}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC       {ECO:0000269|PubMed:3208765}.
CC   -!- TISSUE SPECIFICITY: Hemolymph. {ECO:0000269|PubMed:3208765}.
CC   -!- MISCELLANEOUS: The B chain contains two copper-binding sites
CC       (PubMed:2585484). Three histidine residues are ligands to each copper
CC       ion (PubMed:2585484). {ECO:0000269|PubMed:2585484}.
CC   -!- SIMILARITY: Belongs to the tyrosinase family. Hemocyanin subfamily.
CC       {ECO:0000305}.
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DR   PIR; S02707; BHLOB.
DR   AlphaFoldDB; P10787; -.
DR   SMR; P10787; -.
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..657
FT                   /note="Hemocyanin B chain"
FT                   /id="PRO_0000204292"
FT   BINDING         194
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000269|PubMed:2585484"
FT   BINDING         198
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000269|PubMed:2585484"
FT   BINDING         224
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000269|PubMed:2585484"
FT   BINDING         344
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000269|PubMed:2585484"
FT   BINDING         348
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000269|PubMed:2585484"
FT   BINDING         384
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000269|PubMed:2585484"
FT   CARBOHYD        167
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        93..98
FT                   /evidence="ECO:0000250|UniProtKB:P04254"
FT   DISULFID        483..502
FT                   /evidence="ECO:0000250|UniProtKB:P04254"
FT   DISULFID        562..609
FT                   /evidence="ECO:0000269|PubMed:2585484"
FT   VARIANT         32
FT                   /note="D -> E (in minor component B')"
FT   VARIANT         49
FT                   /note="H -> Q (in minor component B')"
FT   VARIANT         122
FT                   /note="S -> G (in minor component B')"
FT   VARIANT         130
FT                   /note="D -> K (in minor component B')"
FT   VARIANT         132
FT                   /note="I -> V (in minor component B')"
FT   VARIANT         561
FT                   /note="S -> A (in minor component B')"
SQ   SEQUENCE   657 AA;  75392 MW;  D2445E265BC6C47E CRC64;
     DALGTGNANK QQDINHLLDK IYEPTKYPDL KDIAENFNPL GDTSIYNDHG AAAEALMKEL
     NDHRLLEQRH WFSLFNTRQR EEALMLFAVL NQCKEWYCFR SNAAYFRERM NEGEFVYALY
     VSVIHSKLGD GIVLPPLYEI TPHMFTNSEV IDKAYSAKMT QKPGTFNVSF TGTKKNREQR
     VAYFGEDIGM NIHHVTWHMD FPTWWQDSYG YHLDRKGELF FWVHHQLTAR FDFERLSNWL
     DPVDELHWDR IIREGFAPLT SYKYGGEFPV RPDNIHFEDV DGVAHVHDLE ITESRIHDAI
     DHGYITDSDG HTIDIRQPKG IELLGDIIES SMYSSNVQYY GSLHNTAHAM LGRQGDPHGK
     FNLPPGVMEH FETATRDPSF FRLHKYMDNI FKKHTDSFPP YTHDDLEFAG MVVDGIAIDG
     ELITFFDEFQ YSILNAVDSG ENIEDVDINA RVHRLNHNEF TYKITMSNNN DGERLATFRI
     FLCPIEDNNG ITLTLDEARW FCIELDKFFQ KVPSGPETIE RSSKDSSVTV PDMPSFQSLK
     EQADNAVNGG HDLDLSAYER SCGIPDRMLL PKSKPEGMKF NLYVAVTDGD KDTEGHNGGH
     DYGGTHAQCG VHGEAFPDNR PLGYPLERRI PDERVIDGVS NIKHVVVKIV HHLEHHD