HCY2A_RAPVE
ID HCY2A_RAPVE Reviewed; 407 AA.
AC P80960; Q9TWE6;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-MAY-2003, sequence version 2.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Hemocyanin type 2 unit a;
DE AltName: Full=Hemocyanin RHSS2 subunit;
DE AltName: Full=Hemocyanin Rta;
DE AltName: Full=Hemocyanin heavy structural subunit;
DE AltName: Full=RtH2-a;
OS Rapana venosa (Veined rapa whelk) (Rapana thomasiana).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Neogastropoda; Muricoidea; Muricidae; Rapana.
OX NCBI_TaxID=55521;
RN [1]
RP PROTEIN SEQUENCE, AND GLYCOSYLATION AT ASN-27 AND ASN-250.
RC TISSUE=Hemolymph;
RX PubMed=9299521; DOI=10.1006/bbrc.1997.7314;
RA Stoeva S., Idakieva K., Genov N., Voelter W.;
RT "Complete amino acid sequence of dioxygen-binding functional unit of the
RT Rapana thomasiana hemocyanin.";
RL Biochem. Biophys. Res. Commun. 238:403-410(1997).
RN [2]
RP PROTEIN SEQUENCE OF 1-130; 159-217 AND 220-407, AND GLYCOSYLATION.
RC TISSUE=Hemolymph;
RX PubMed=9180018; DOI=10.1016/s0305-0491(96)00292-1;
RA Stoeva S., Idakieva K., Rachev R., Voelter W., Genov N.;
RT "Amino-terminal oxygen-binding functional unit of the Rapana thomasiana
RT grosse (gastropod) hemocyanin: carbohydrate content, monosaccharide
RT composition and amino acid sequence studies.";
RL Comp. Biochem. Physiol. 117B:101-107(1997).
RN [3]
RP PROTEIN SEQUENCE OF 1-25, AND MASS SPECTROMETRY.
RX PubMed=8590374; DOI=10.1016/0305-0491(95)00102-6;
RA Idakieva K., Stoeva S., Voelter W., Genov N.;
RT "Functional unit of the Rapana thomasiana (Grosse) (marine snail,
RT gastropod) hemocyanin.";
RL Comp. Biochem. Physiol. 112B:599-606(1995).
RN [4]
RP SUBUNIT.
RX PubMed=11004539; DOI=10.1016/s0167-4838(00)00053-4;
RA Idakieva K., Stoeva S., Pervanova K., Genov N., Voelter W.;
RT "Arrangement of functional units within the Rapana thomasiana hemocyanin
RT subunit RtH2.";
RL Biochim. Biophys. Acta 1479:175-184(2000).
CC -!- FUNCTION: Hemocyanins are copper-containing oxygen carriers occurring
CC freely dissolved in the hemolymph of many mollusks and arthropods.
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000250};
CC Note=Binds 2 copper ions per heterodimer. {ECO:0000250};
CC -!- SUBUNIT: Decamers of large identical subunits, each containing 8
CC globular oxygen-binding functional units.
CC {ECO:0000269|PubMed:11004539}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC -!- TISSUE SPECIFICITY: Hemolymph.
CC -!- MASS SPECTROMETRY: Mass=49698; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:8590374};
CC -!- SIMILARITY: Belongs to the tyrosinase family. Hemocyanin subfamily.
CC {ECO:0000305}.
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DR AlphaFoldDB; P80960; -.
DR SMR; P80960; -.
DR iPTMnet; P80960; -.
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; 2.60.310.10; -; 1.
DR InterPro; IPR008922; Di-copper_centre_dom_sf.
DR InterPro; IPR028999; Haemocyanin_beta-sandwich.
DR InterPro; IPR036848; Haemocyanin_C_sf.
DR InterPro; IPR002227; Tyrosinase_Cu-bd.
DR Pfam; PF14830; Haemocyan_bet_s; 1.
DR Pfam; PF00264; Tyrosinase; 2.
DR PRINTS; PR00092; TYROSINASE.
DR SUPFAM; SSF48056; SSF48056; 1.
DR SUPFAM; SSF81277; SSF81277; 1.
DR PROSITE; PS00497; TYROSINASE_1; 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; Thioether bond; Transport.
FT CHAIN 1..407
FT /note="Hemocyanin type 2 unit a"
FT /id="PRO_0000204306"
FT BINDING 41
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT BINDING 70
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT BINDING 171
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT BINDING 175
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT BINDING 202
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT CARBOHYD 27
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:9299521"
FT CARBOHYD 250
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:9299521"
FT DISULFID 47..58
FT /evidence="ECO:0000250"
FT DISULFID 161..228
FT /evidence="ECO:0000250"
FT DISULFID 319..325
FT /evidence="ECO:0000250"
FT CROSSLNK 59..61
FT /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT /evidence="ECO:0000250"
FT CONFLICT 22
FT /note="M -> L (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 407 AA; 46756 MW; CE5ABCF2E385AF14 CRC64;
SLLRKNVDSL TEEEILTLQS VMRELQNDSS EHGFQSIASF HGSPPLCPSP EANKKVACCV
HGMASFPQWH RIFTKQMEAA LMGHGAKVGM PYWDWTTSFT KLPRFIPYDD EQLNPFVRIT
DLEDHFTTRD PQPELFKDPE GGDESFFFRQ VLIALEQRDY CDFEVQFEVI HNSIHYWIGG
HQKYGMSTLE YTAYDPLFFI HHSNVDRLWA IWQELQKYRG LPYDESDCGV ELMREPLQPF
AQTSATNPNN VTRAHSTPKS LFNYRQLAGY TYDTLTLNGM TISQLESSLL RLQKEEDRVF
AGFLLRGIGS SADVTFDLCD KDEHCDFAGT FAVLGGPLEM PWSFDRLFKM DVTKVFKQMR
LRPDDSEYHF ELEVTARAGT DLSPELLKPG SVSFLPGRKI QNTPDVR
