HCY2_LIMPO
ID HCY2_LIMPO Reviewed; 628 AA.
AC P04253;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 2.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Hemocyanin II;
OS Limulus polyphemus (Atlantic horseshoe crab).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Merostomata;
OC Xiphosura; Limulidae; Limulus.
OX NCBI_TaxID=6850;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=3525550; DOI=10.1016/s0021-9258(18)67416-2;
RA Nakashima H., Behrens P.Q., Moore M.D., Yokota E., Riggs A.F.;
RT "Structure of hemocyanin II from the horseshoe crab, Limulus polyphemus.
RT Sequences of the overlapping peptides, ordering the CNBr fragments, and the
RT complete amino acid sequence.";
RL J. Biol. Chem. 261:10526-10533(1986).
RN [2]
RP PROTEIN SEQUENCE OF 1-203.
RX PubMed=6715319; DOI=10.1016/s0021-9258(17)42909-7;
RA Yokota E., Riggs A.F.;
RT "The structure of the hemocyanin from the horseshoe crab, Limulus
RT polyphemus. The amino acid sequence of the largest cyanogen bromide
RT fragment.";
RL J. Biol. Chem. 259:4739-4749(1984).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX PubMed=1866430; DOI=10.1002/prot.340090403;
RA Magnus K.A., Lattman E.E., Volbeda A., Hol W.G.J.;
RT "Hexamers of subunit II from Limulus hemocyanin (a 48-mer) have the same
RT quaternary structure as whole Panulirus hemocyanin molecules.";
RL Proteins 9:240-247(1991).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.18 ANGSTROMS).
RX PubMed=8518732; DOI=10.1002/pro.5560020411;
RA Hazes B., Magnus K.A., Bonaventura C., Bonaventura J., Dauter Z.,
RA Kalk K.H., Hol W.G.J.;
RT "Crystal structure of deoxygenated Limulus polyphemus subunit II hemocyanin
RT at 2.18-A resolution: clues for a mechanism for allosteric regulation.";
RL Protein Sci. 2:597-619(1993).
CC -!- FUNCTION: Hemocyanins are copper-containing oxygen carriers occurring
CC freely dissolved in the hemolymph of many mollusks and arthropods.
CC -!- SUBUNIT: Hexamer or a multiple thereof.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC -!- TISSUE SPECIFICITY: Hemolymph.
CC -!- SIMILARITY: Belongs to the tyrosinase family. Hemocyanin subfamily.
CC {ECO:0000305}.
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DR PIR; A26713; BHHC2A.
DR PDB; 1LL1; X-ray; 2.55 A; A=1-628.
DR PDB; 1LLA; X-ray; 2.18 A; A=1-628.
DR PDB; 1NOL; X-ray; 2.40 A; A=1-628.
DR PDB; 1OXY; X-ray; 2.40 A; A=1-628.
DR PDBsum; 1LL1; -.
DR PDBsum; 1LLA; -.
DR PDBsum; 1NOL; -.
DR PDBsum; 1OXY; -.
DR AlphaFoldDB; P04253; -.
DR SMR; P04253; -.
DR EvolutionaryTrace; P04253; -.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0031404; F:chloride ion binding; IDA:UniProtKB.
DR GO; GO:0005507; F:copper ion binding; IDA:UniProtKB.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0005344; F:oxygen carrier activity; NAS:UniProtKB.
DR GO; GO:0015671; P:oxygen transport; NAS:UniProtKB.
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..628
FT /note="Hemocyanin II"
FT /id="PRO_0000204281"
FT BINDING 173
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:8518732"
FT BINDING 177
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:8518732"
FT BINDING 204
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:8518732"
FT BINDING 324
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:8518732"
FT BINDING 328
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:8518732"
FT BINDING 364
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:8518732"
FT MOD_RES 1
FT /note="Blocked amino end (Thr); partial"
FT /evidence="ECO:0000269|PubMed:3525550"
FT CARBOHYD 449
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 534..576
FT DISULFID 536..583
FT HELIX 3..13
FT /evidence="ECO:0007829|PDB:1LLA"
FT HELIX 16..18
FT /evidence="ECO:0007829|PDB:1LLA"
FT HELIX 33..36
FT /evidence="ECO:0007829|PDB:1LLA"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:1LLA"
FT HELIX 51..65
FT /evidence="ECO:0007829|PDB:1LLA"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:1OXY"
FT HELIX 70..80
FT /evidence="ECO:0007829|PDB:1LLA"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:1LLA"
FT HELIX 86..99
FT /evidence="ECO:0007829|PDB:1LLA"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:1LLA"
FT HELIX 111..114
FT /evidence="ECO:0007829|PDB:1LLA"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:1LLA"
FT HELIX 122..130
FT /evidence="ECO:0007829|PDB:1LLA"
FT STRAND 143..146
FT /evidence="ECO:0007829|PDB:1LLA"
FT HELIX 156..160
FT /evidence="ECO:0007829|PDB:1LLA"
FT HELIX 161..164
FT /evidence="ECO:0007829|PDB:1LLA"
FT HELIX 167..179
FT /evidence="ECO:0007829|PDB:1LLA"
FT HELIX 186..189
FT /evidence="ECO:0007829|PDB:1LLA"
FT HELIX 196..217
FT /evidence="ECO:0007829|PDB:1LLA"
FT TURN 243..245
FT /evidence="ECO:0007829|PDB:1LLA"
FT HELIX 266..282
FT /evidence="ECO:0007829|PDB:1LLA"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:1LLA"
FT STRAND 292..294
FT /evidence="ECO:0007829|PDB:1LLA"
FT TURN 297..299
FT /evidence="ECO:0007829|PDB:1LLA"
FT HELIX 300..309
FT /evidence="ECO:0007829|PDB:1LLA"
FT HELIX 317..320
FT /evidence="ECO:0007829|PDB:1LLA"
FT HELIX 323..332
FT /evidence="ECO:0007829|PDB:1LLA"
FT TURN 333..335
FT /evidence="ECO:0007829|PDB:1LLA"
FT HELIX 347..349
FT /evidence="ECO:0007829|PDB:1LLA"
FT TURN 351..353
FT /evidence="ECO:0007829|PDB:1LLA"
FT HELIX 354..356
FT /evidence="ECO:0007829|PDB:1LLA"
FT HELIX 358..375
FT /evidence="ECO:0007829|PDB:1LLA"
FT HELIX 383..386
FT /evidence="ECO:0007829|PDB:1LLA"
FT STRAND 391..402
FT /evidence="ECO:0007829|PDB:1LLA"
FT STRAND 405..416
FT /evidence="ECO:0007829|PDB:1LLA"
FT TURN 418..420
FT /evidence="ECO:0007829|PDB:1LLA"
FT STRAND 429..438
FT /evidence="ECO:0007829|PDB:1LLA"
FT STRAND 442..449
FT /evidence="ECO:0007829|PDB:1LLA"
FT STRAND 451..453
FT /evidence="ECO:0007829|PDB:1LLA"
FT STRAND 455..467
FT /evidence="ECO:0007829|PDB:1LLA"
FT HELIX 476..482
FT /evidence="ECO:0007829|PDB:1LLA"
FT STRAND 484..493
FT /evidence="ECO:0007829|PDB:1LLA"
FT STRAND 495..503
FT /evidence="ECO:0007829|PDB:1LLA"
FT HELIX 504..506
FT /evidence="ECO:0007829|PDB:1LLA"
FT STRAND 510..512
FT /evidence="ECO:0007829|PDB:1NOL"
FT HELIX 517..521
FT /evidence="ECO:0007829|PDB:1LLA"
FT STRAND 537..539
FT /evidence="ECO:0007829|PDB:1LLA"
FT HELIX 540..542
FT /evidence="ECO:0007829|PDB:1LLA"
FT STRAND 548..550
FT /evidence="ECO:0007829|PDB:1OXY"
FT STRAND 552..562
FT /evidence="ECO:0007829|PDB:1LLA"
FT HELIX 563..566
FT /evidence="ECO:0007829|PDB:1LLA"
FT HELIX 580..583
FT /evidence="ECO:0007829|PDB:1LLA"
FT TURN 596..599
FT /evidence="ECO:0007829|PDB:1LLA"
FT STRAND 600..602
FT /evidence="ECO:0007829|PDB:1LLA"
FT STRAND 606..608
FT /evidence="ECO:0007829|PDB:1LLA"
FT HELIX 609..611
FT /evidence="ECO:0007829|PDB:1LLA"
FT STRAND 617..626
FT /evidence="ECO:0007829|PDB:1LLA"
SQ SEQUENCE 628 AA; 72629 MW; 6B8B4C6D8B1225BE CRC64;
TLHDKQIRVC HLFEQLSSAT VIGDGDKHKH SDRLKNVGKL QPGAIFSCFH PDHLEEARHL
YEVFWEAGDF NDFIEIAKEA RTFVNEGLFA FAAEVAVLHR DDCKGLYVPP VQEIFPDKFI
PSAAINEAFK KAHVRPEFDE SPILVDVQDT GNILDPEYRL AYYREDVGIN AHHWHWHLVY
PSTWNPKYFG KKKDRKGELF YYMHQQMCAR YDCERLSNGM HRMLPFNNFD EPLAGYAPHL
THVASGKYYS PRPDGLKLRD LGDIEISEMV RMRERILDSI HLGYVISEDG SHKTLDELHG
TDILGALVES SYESVNHEYY GNLHNWGHVT MARIHDPDGR FHEEPGVMSD TSTSLRDPIF
YNWHRFIDNI FHEYKNTLKP YDHDVLNFPD IQVQDVTLHA RVDNVVHFTM REQELELKHG
INPGNARSIK ARYYHLDHEP FSYAVNVQNN SASDKHATVR IFLAPKYDEL GNEIKADELR
RTAIELDKFK TDLHPGKNTV VRHSLDSSVT LSHQPTFEDL LHGVGLNEHK SEYCSCGWPS
HLLVPKGNIK GMEYHLFVML TDWDKDKVDG SESVACVDAV SYCGARDHKY PDKKPMGFPF
DRPIHTEHIS DFLTNNMFIK DIKIKFHE
