HCY_PALVU
ID HCY_PALVU Reviewed; 657 AA.
AC P80888;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2003, sequence version 2.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Hemocyanin;
OS Palinurus vulgaris (European spiny lobster).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Achelata;
OC Palinuroidea; Palinuridae; Palinurus.
OX NCBI_TaxID=6733;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=8939004; DOI=10.1016/0305-0491(96)00119-8;
RA Jekel P.A., Neuteboom B., Beintema J.J.;
RT "Primary structure of hemocyanin from Palinurus vulgaris.";
RL Comp. Biochem. Physiol. 115B:243-246(1996).
CC -!- FUNCTION: Hemocyanins are copper-containing oxygen carriers occurring
CC freely dissolved in the hemolymph of many mollusks and arthropods.
CC -!- SUBUNIT: It consists of at least four very similar subunits.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC -!- TISSUE SPECIFICITY: Hemolymph.
CC -!- SIMILARITY: Belongs to the tyrosinase family. Hemocyanin subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: The sequence has been determined from a mixture of all the
CC subunits and so the exact sequence as well as the relevance of the
CC variants described is unknown for each subunit. {ECO:0000305}.
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DR AlphaFoldDB; P80888; -.
DR SMR; P80888; -.
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; 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"
FT /id="PRO_0000204290"
FT BINDING 194
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT BINDING 198
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT BINDING 224
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT BINDING 344
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT BINDING 348
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT BINDING 384
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT CARBOHYD 167
FT /note="N-linked (GlcNAc...) asparagine"
FT DISULFID 483..502
FT DISULFID 562..609
FT VARIANT 24
FT /note="P -> D (depending on subunit)"
FT VARIANT 26
FT /note="K -> E (depending on subunit)"
FT VARIANT 29
FT /note="K -> E (depending on subunit)"
FT VARIANT 38..39
FT /note="NP -> DE (depending on subunit)"
FT VARIANT 59
FT /note="K -> E (depending on subunit)"
FT VARIANT 80
FT /note="R -> H (depending on subunit)"
FT VARIANT 84
FT /note="A -> E (depending on subunit)"
FT VARIANT 84
FT /note="A -> Q (depending on subunit)"
FT VARIANT 174
FT /note="Q -> K (depending on subunit)"
FT VARIANT 177
FT /note="R -> K (depending on subunit)"
FT VARIANT 275..276
FT /note="TH -> IR (depending on subunit)"
FT VARIANT 287
FT /note="R -> H (depending on subunit)"
FT VARIANT 294
FT /note="N -> S (depending on subunit)"
FT VARIANT 414..418
FT /note="DNIAI -> NGVPL (depending on subunit)"
FT VARIANT 421
FT /note="H -> R (depending on subunit)"
FT VARIANT 423
FT /note="T -> I (depending on subunit)"
FT VARIANT 444
FT /note="E -> K (depending on subunit)"
FT VARIANT 447
FT /note="E -> A (depending on subunit)"
FT VARIANT 463
FT /note="D -> E (depending on subunit)"
FT VARIANT 463
FT /note="D -> I (depending on subunit)"
FT VARIANT 465
FT /note="E -> D (depending on subunit)"
FT VARIANT 467
FT /note="R -> L (depending on subunit)"
FT VARIANT 467
FT /note="R -> S (depending on subunit)"
FT VARIANT 469
FT /note="H -> N (depending on subunit)"
FT VARIANT 471
FT /note="E -> D (depending on subunit)"
FT VARIANT 474
FT /note="K -> H (depending on subunit)"
FT VARIANT 615
FT /note="L -> Q (depending on subunit)"
FT VARIANT 626
FT /note="L -> S (depending on subunit)"
FT VARIANT 652
FT /note="D -> N (depending on subunit)"
SQ SEQUENCE 657 AA; 75674 MW; F52C819BA6E0ADD3 CRC64;
DVHSSDNAHK QHDVNHLLDK IYEPIKDEKL HNTAHTFNPV ADTSIYGDDG AAAKTLMQKL
NDHRLLEEHH WFSLFNTRQR EELAMLFTVL NQCKEWDFLN NNAAFFRERM NEGEFVYALY
VSVIHSKLGD GIVLPPLYQI TPHMFTNSEV IDKAYSAKMT HKEGTFNMSF TGTQKNREQR
VAYFGQDIGM NIHHVTWHMD FPFWWDDSYG YHLDRKGELF FWVHHQLTAR FDAERFSNWM
DPVDELHWDD IIHEGFAPHA SYKYGGEFPT RPDNTHFKNV DGVARVRDME ITENRIRDAI
AHGYITATDG HTIDIRQPNG IELLGDIIES SMYSSNPHYP GSLHNTAHGM LGRQGDPHGK
FNMPPGVMEH FETATRDPSF FRLHKYMDNI FKEHTDSFPP YTHEDLEFPG VSVDNIAIEG
HLTTFFDQFK YSLVNAVDSG ENVEDVEIYA NVHRLNHEEF TYDIEVRNHN EEDKFATVRI
FLCPTEDNNG ITLNLDEARW LCLELDKFWT KLGDGKNLIE RSSKDSSVTV PDMPSFESLK
KQADEAVNGG HDLDLSAYER SCGIPDRMLL PKSKPQGMEF NLYVAVTDGD KDTDGSHGDH
DHHGTHAQCG IHGELYPDHR PLGYPLERRI PDDRVFDGVS NIKHALVKIV HDPELRA
