HCY2E_RAPVE
ID HCY2E_RAPVE Reviewed; 413 AA.
AC P83040;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Hemocyanin type 2 unit e;
DE AltName: Full=RtH2-e;
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-17 AND ASN-127.
RC TISSUE=Hemolymph;
RX PubMed=11888200; DOI=10.1006/abbi.2001.2741;
RA Stoeva S., Idakieva K., Betzel C., Genov N., Voelter W.;
RT "Amino acid sequence and glycosylation of functional unit RtH2-e from
RT Rapana thomasiana (gastropod) hemocyanin.";
RL Arch. Biochem. Biophys. 399:149-158(2002).
RN [2]
RP CRYSTALLIZATION.
RX PubMed=11679737; DOI=10.1107/s0907444901012124;
RA Perbandt M., Chandra V., Rajashankar K.R., Idakieva K., Parvanova K.,
RA Rypniewski W., Stoeva S., Voelter W., Genov N., Betzel C.;
RT "Preliminary X-ray diffraction studies of the external functional unit
RT RtH2-e from the Rapana thomasiana.";
RL Acta Crystallogr. D 57:1663-1665(2001).
RN [3]
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).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 6-413, DISULFIDE BOND, AND
RP THIOETHER BOND.
RX PubMed=12767214; DOI=10.1021/bi020672x;
RA Perbandt M., Guthoehrlein E.W., Rypniewski W., Idakieva K., Stoeva S.,
RA Voelter W., Genov N., Betzel C.;
RT "The structure of a functional unit from the wall of a gastropod hemocyanin
RT offers a possible mechanism for cooperativity.";
RL Biochemistry 42:6341-6346(2003).
CC -!- FUNCTION: Hemocyanins are copper-containing oxygen carriers occurring
CC freely dissolved in the hemolymph of many mollusks and arthropods.
CC {ECO:0000250|UniProtKB:P12659}.
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Note=Binds 2 copper ions per heterodimer.;
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. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the tyrosinase family. Hemocyanin subfamily.
CC {ECO:0000305}.
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DR PDB; 1LNL; X-ray; 3.30 A; A/B/C=7-413.
DR PDBsum; 1LNL; -.
DR AlphaFoldDB; P83040; -.
DR SMR; P83040; -.
DR iPTMnet; P83040; -.
DR PRIDE; P83040; -.
DR EvolutionaryTrace; P83040; -.
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; 1.
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 3D-structure; Copper; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Metal-binding; Oxygen transport; Secreted; Thioether bond;
KW Transport.
FT CHAIN 1..413
FT /note="Hemocyanin type 2 unit e"
FT /id="PRO_0000204307"
FT BINDING 49
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT BINDING 69
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT BINDING 78
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT BINDING 189
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT BINDING 193
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT BINDING 220
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT CARBOHYD 17
FT /note="N-linked (GlcNAc...) (high mannose) asparagine"
FT /evidence="ECO:0000269|PubMed:11888200"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) (high mannose) asparagine"
FT /evidence="ECO:0000269|PubMed:11888200"
FT DISULFID 55..66
FT /evidence="ECO:0000269|PubMed:12767214,
FT ECO:0007744|PDB:1LNL"
FT DISULFID 179..246
FT /evidence="ECO:0000269|PubMed:12767214,
FT ECO:0007744|PDB:1LNL"
FT DISULFID 336..342
FT /evidence="ECO:0000269|PubMed:12767214,
FT ECO:0007744|PDB:1LNL"
FT CROSSLNK 67..69
FT /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT /evidence="ECO:0000269|PubMed:12767214"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:1LNL"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:1LNL"
FT HELIX 20..33
FT /evidence="ECO:0007829|PDB:1LNL"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:1LNL"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:1LNL"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:1LNL"
FT HELIX 74..91
FT /evidence="ECO:0007829|PDB:1LNL"
FT HELIX 112..115
FT /evidence="ECO:0007829|PDB:1LNL"
FT TURN 122..125
FT /evidence="ECO:0007829|PDB:1LNL"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:1LNL"
FT HELIX 164..173
FT /evidence="ECO:0007829|PDB:1LNL"
FT HELIX 179..197
FT /evidence="ECO:0007829|PDB:1LNL"
FT STRAND 201..203
FT /evidence="ECO:0007829|PDB:1LNL"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:1LNL"
FT HELIX 215..219
FT /evidence="ECO:0007829|PDB:1LNL"
FT HELIX 222..236
FT /evidence="ECO:0007829|PDB:1LNL"
FT TURN 248..252
FT /evidence="ECO:0007829|PDB:1LNL"
FT HELIX 258..260
FT /evidence="ECO:0007829|PDB:1LNL"
FT TURN 262..264
FT /evidence="ECO:0007829|PDB:1LNL"
FT HELIX 268..271
FT /evidence="ECO:0007829|PDB:1LNL"
FT HELIX 276..279
FT /evidence="ECO:0007829|PDB:1LNL"
FT HELIX 282..285
FT /evidence="ECO:0007829|PDB:1LNL"
FT STRAND 288..291
FT /evidence="ECO:0007829|PDB:1LNL"
FT STRAND 295..297
FT /evidence="ECO:0007829|PDB:1LNL"
FT HELIX 300..310
FT /evidence="ECO:0007829|PDB:1LNL"
FT STRAND 315..320
FT /evidence="ECO:0007829|PDB:1LNL"
FT STRAND 329..336
FT /evidence="ECO:0007829|PDB:1LNL"
FT STRAND 338..340
FT /evidence="ECO:0007829|PDB:1LNL"
FT STRAND 342..350
FT /evidence="ECO:0007829|PDB:1LNL"
FT STRAND 365..368
FT /evidence="ECO:0007829|PDB:1LNL"
FT HELIX 370..374
FT /evidence="ECO:0007829|PDB:1LNL"
FT TURN 375..377
FT /evidence="ECO:0007829|PDB:1LNL"
FT STRAND 385..395
FT /evidence="ECO:0007829|PDB:1LNL"
FT HELIX 400..402
FT /evidence="ECO:0007829|PDB:1LNL"
SQ SEQUENCE 413 AA; 47963 MW; 99A8EAB3426F949E CRC64;
DDQGHTHRNL VRKSVRNLSP AERRSLVHAL KSLQEDSSAD GFQSLASFHA QPPLCPYPEA
NKRFACCVHG MATFPEWHRL YTVQFEDALR RHGSVVGIPY WDTVVPQEDL PAFFNDEIWD
DPLFHANFTN PFNGADIDFN HQKIARDINV DKLFKEGPKG YDTWSFKQYI YALEQEDYCD
FEVQFEIAHN AIHAWVGGTE EYSMGHLHYA SYDPVFILHH SNTDRLFALW QELQKFRGHD
PNEVNCALEM MREPLKPFSF GAPYNLNPTT KEHSKPEDTF DYKGHFHYEY DHLELQGMNV
QRLHDYINQQ KERDRVFAGF LLEGIGTSAH LDFSICKIDG ECTHAGYFDV LGGSLETPWQ
FDRLYKYEIT DVLESKGLDV HDVFDIKITQ TSWDNEDIST DRFPPPSVIY VPK
