HCYB_ASTLP
ID HCYB_ASTLP Reviewed; 566 AA.
AC P83180;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Hemocyanin B chain;
OS Astacus leptodactylus (Turkish narrow-clawed crayfish) (Pontastacus
OS leptodactylus).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Astacidea;
OC Astacoidea; Astacidae; Astacus.
OX NCBI_TaxID=6717 {ECO:0000305};
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE.
RC TISSUE=Blood;
RA Schneider H.-J., Voll W., Lehmann L., Grisshammer R., Goettgens A.,
RA Linzen B.;
RT "Partial amino acid sequence of crayfish (Astacus Leptodactylus)
RT hemocyanin.";
RL (In) Linzen B. (eds.);
RL Invertebrate Oxygen Carriers, pp.173-176, Springer-Verlag, Heidelberg
RL (1986).
CC -!- FUNCTION: Hemocyanins are copper-containing oxygen carriers occurring
CC freely dissolved in the hemolymph of many mollusks and arthropods.
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC -!- TISSUE SPECIFICITY: Hemolymph.
CC -!- MISCELLANEOUS: The B chain contains two copper-binding sites. Three
CC histidine residues are ligands to each copper ion. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the tyrosinase family. Hemocyanin subfamily.
CC {ECO:0000305}.
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DR AlphaFoldDB; P83180; -.
DR SMR; P83180; -.
DR GlyConnect; 212; 6 N-Linked glycans.
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; Metal-binding;
KW Oxygen transport; Secreted; Transport.
FT CHAIN 1..566
FT /note="Hemocyanin B chain"
FT /id="PRO_0000204298"
FT BINDING 183
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT BINDING 187
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT BINDING 213
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT BINDING 309
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT BINDING 313
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT BINDING 347
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT DISULFID 82..87
FT /evidence="ECO:0000250"
FT VARIANT 42
FT /note="A -> D"
FT /evidence="ECO:0000305"
FT VARIANT 146
FT /note="A -> G"
FT /evidence="ECO:0000305"
FT VARIANT 235
FT /note="I -> G"
FT /evidence="ECO:0000305"
FT VARIANT 447
FT /note="D -> A"
FT /evidence="ECO:0000305"
FT UNSURE 45
FT /note="I or L"
FT UNSURE 50
FT /evidence="ECO:0000305"
FT UNSURE 74
FT /evidence="ECO:0000305"
FT UNSURE 108
FT /note="I or L"
FT UNSURE 113
FT /note="I or L"
FT UNSURE 117
FT /note="I or L"
FT UNSURE 121
FT /note="I or L"
FT UNSURE 123
FT /note="I or L"
FT UNSURE 126
FT /note="I or L"
FT UNSURE 133
FT /note="I or L"
FT UNSURE 140
FT /note="I or L"
FT UNSURE 225
FT /note="I or L"
FT UNSURE 229
FT /note="I or L"
FT UNSURE 235
FT /note="I or L"
FT UNSURE 308
FT /note="I or L"
FT UNSURE 314
FT /note="I or L"
FT UNSURE 316
FT /note="I or L"
FT UNSURE 369
FT /note="I or L"
FT UNSURE 376
FT /note="I or L"
FT UNSURE 410
FT /note="I or L"
FT UNSURE 419
FT /note="I or L"
FT UNSURE 421
FT /note="I or L"
FT UNSURE 427
FT /note="I or L"
FT UNSURE 429
FT /note="I or L"
FT UNSURE 446
FT /note="I or L"
FT UNSURE 453
FT /note="I or L"
FT UNSURE 488
FT /note="I or L"
FT UNSURE 489
FT /note="I or L"
FT UNSURE 490
FT /note="I or L"
FT UNSURE 511
FT /note="I or L"
FT UNSURE 518
FT /evidence="ECO:0000305"
FT UNSURE 520
FT /note="I or L"
SQ SEQUENCE 566 AA; 65289 MW; F3DF4FDE3B87DFBD CRC64;
DASGATLAKR QQVVNHLLEH IYDHTHFTDL KNIAGTFSPE AATSIYTDDM EELRDGRLLE
QHHWFSLFNT RQRMLFEVLI HCKSWECFLD NAAYFRERMN EGEFVYAIYV AVIHSGIGHG
IVIPPIYEVT PHIFTNSEVI NKAYSAKMTQ TPGRFNMDFT GTKKNKEQRV AYFGEDIGMN
IHHVTWHMDF PFWWKDSYGY HLDRKGELFF WVHHQLTARF DSERISNWID VVDEIHWSCI
EGFAPHTSYK YGGEFPARPD NVHFEDVDGV ARVRDSRIRD ALAHGYLLDN SGNKSSVYSP
NVQYYGAIHN TAHIMIGRQG DHKFDMPPGV MEHFETATRD PSFFRLHKYM DNIFKEHKDS
LPPYTKNDIA VPGVVIDSVA QLKTFFDTFE VNLGNAKVAD VAISADVHRI NHEEFSYNID
ISNTDKIFIC PVKDDNGIMD KFYKSIDPGT NHIVRKSVDS SVTVPDRQYA LDLHMFERSC
GIPNRDMIII ESRPDGMDFA LFVTVDDPEE IGATHSQHGI KKYPDKKPMG YPVDRSIPDN
RVFLESPNIK RTYVKVFHDE HGGEQH
