ID   HC2C_MEGCR              Reviewed;         420 AA.
AC   P81732;
DT   29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Hemocyanin 2-c chain;
DE   AltName: Full=KLH2-c;
OS   Megathura crenulata (Giant keyhole limpet).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Vetigastropoda; Lepetellida; Fissurelloidea; Fissurellidae; Megathura.
OX   NCBI_TaxID=55429;
RN   [1]
RP   PROTEIN SEQUENCE, AND MASS SPECTROMETRY.
RC   TISSUE=Hemolymph;
RX   PubMed=10561541; DOI=10.1016/s0167-4838(99)00198-3;
RA   Stoeva S., Schuetz J., Gebauer W., Hundsdoerfer T., Manz C., Markl J.,
RA   Voelter W.;
RT   "Primary structure and unusual carbohydrate moiety of functional unit 2-c
RT   of keyhole limpet hemocyanin (KLH).";
RL   Biochim. Biophys. Acta 1435:94-109(1999).
CC   -!- FUNCTION: Hemocyanins are copper-containing oxygen carriers occurring
CC       freely dissolved in the hemolymph of many mollusks and arthropods.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Hemolymph.
CC   -!- PTM: O-glycosylated.
CC   -!- MASS SPECTROMETRY: Mass=56126; Mass_error=150; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:10561541};
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DR   AlphaFoldDB; P81732; -.
DR   SMR; P81732; -.
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   Copper; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Metal-binding; Oxygen transport; Secreted; Transport.
FT   CHAIN           1..420
FT                   /note="Hemocyanin 2-c chain"
FT                   /id="PRO_0000204289"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         46
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250"
FT   BINDING         66
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250"
FT   BINDING         73
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250"
FT   BINDING         185
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250"
FT   BINDING         189
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250"
FT   BINDING         216
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250"
FT   DISULFID        52..63
FT                   /evidence="ECO:0000250"
FT   DISULFID        175..242
FT                   /evidence="ECO:0000250"
FT   DISULFID        335..342
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   420 AA;  48091 MW;  512A99415CCA54B2 CRC64;
     DFGHSKKIRK NVHSLTAEEQ NSLRRAMDDL QDDKTRGGFQ QIAAFHGEPK WCPRPEAEKK
     FACCVHGMAV FPHWHRLLTV QGENALRKHG FTGGLPYWDW TRPMSALPHF VADPTYDDSV
     SSLEEDNPYS HGHIDSVGHD TTRAVRDDLY QSPGFGHYTD IAKQVLLALE QDDFCDFEVQ
     FEIAHNSIHA LVGGNEPYGM STLEYFLYDP IFFLHHSNTD RLWAIWQALQ KYRGKPYNTA
     NCAIVRHDTY RKPLQPFGLD SVINPDDETR EHSVPRDVFN YKDDFNYEYE SLNFNGLSIA
     QLDRELQRIK SHDRVFAGFL LHEIGQSALV KFYVCKHHVS DCDHYAGEFY ILGDEAEMPF
     AYDRVYKYEI SQALHDLDLH VGDNFHLKYE AFNLNGGSLG GVDLSQPSVI FEPAAGSHTA