HCY2_CARAE
ID HCY2_CARAE Reviewed; 650 AA.
AC P84293;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Hemocyanin subunit 2;
DE AltName: Full=CaeSS2;
OS Carcinus aestuarii (Green crab) (Carcinus mediterraneus).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Brachyura;
OC Eubrachyura; Portunoidea; Carcinidae; Carcinus.
OX NCBI_TaxID=53602;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND GLYCOSYLATION AT SER-172 AND ASN-309.
RX PubMed=16169881; DOI=10.1093/jb/mvi130;
RA Dolashka-Angelova P., Dolashki A., Savvides S.N., Hristova R.,
RA Van Beeumen J., Voelter W., Devreese B., Weser U., Di Muro P., Salvato B.,
RA Stevanovic S.;
RT "Structure of hemocyanin subunit CaeSS2 of the crustacean mediterranean
RT crab Carcinus aestuarii.";
RL J. Biochem. 138:303-312(2005).
RN [2]
RP GLYCOSYLATION AT SER-120.
RA Stevanovic S.;
RL Unpublished observations (JAN-2005).
CC -!- FUNCTION: Hemocyanins are copper-containing oxygen carriers occurring
CC freely dissolved in the hemolymph of many mollusks and arthropods.
CC {ECO:0000269|PubMed:16169881, ECO:0000305}.
CC -!- SUBUNIT: Hexamer of a number of different chains, of which five have
CC been identified. {ECO:0000269|PubMed:16169881}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC {ECO:0000269|PubMed:16169881}.
CC -!- TISSUE SPECIFICITY: Hemolymph. {ECO:0000269|PubMed:16169881}.
CC -!- PTM: Contains one N-glycosylated and three O-glycosylated residues. The
CC position of one of the O-glycosylated residues has not been determined.
CC {ECO:0000269|PubMed:16169881}.
CC -!- PTM: O-linked glycan at Ser-120 may be composed of two GalNAc, three
CC Gal, and two N-acetylneuraminic acid units for a total 1525-Da MW.
CC {ECO:0000269|PubMed:16169881, ECO:0000269|Ref.2}.
CC -!- SIMILARITY: Belongs to the tyrosinase family. Hemocyanin subfamily.
CC {ECO:0000255}.
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DR AlphaFoldDB; P84293; -.
DR SMR; P84293; -.
DR iPTMnet; P84293; -.
DR PRIDE; P84293; -.
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; Glycoprotein; Metal-binding;
KW Oxygen transport; Secreted; Transport.
FT CHAIN 1..650
FT /note="Hemocyanin subunit 2"
FT /id="PRO_0000204256"
FT BINDING 193
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:P10787"
FT BINDING 197
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:P10787"
FT BINDING 225
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:P10787"
FT BINDING 344
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:P10787"
FT BINDING 348
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:P10787"
FT BINDING 384
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:P10787"
FT CARBOHYD 120
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|Ref.2"
FT CARBOHYD 172
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:16169881"
FT CARBOHYD 309
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16169881"
FT UNSURE 118
FT /note="S or L"
FT /evidence="ECO:0000269|PubMed:16169881"
FT UNSURE 120
FT /note="S or V"
FT /evidence="ECO:0000269|PubMed:16169881"
SQ SEQUENCE 650 AA; 75035 MW; 9013624F39162528 CRC64;
DSPGGASDAQ KTFDVNSLMP VKYEEIRDPH LKELSLSFDP LSGHYDDDGV SAKRLMKELN
EHRLLQQSHW FSLFNPRTRE EDLMLYNVDE HSGNWDTFAG NAAFFRVHVN EGFFVYASYS
VVIHSKLTQH VVLPPLYEVT PHLFTNSEVI QKAYAAKMTQ TPTKIFAHFT GSKSNPEQRV
AYFGEDIGMN THHVTWHLEF PFWWDDAHYD HHIERKGESC SSWVHHQLTV RFDAERLSNY
LDPVRELHWD DVIHEGFAPH TSYKYGGYFP DRPDNVNFED VDGVARVRDM LLFEERIQDA
IAHGYLRYNG STINIRDNHG IDVLGDVFES SMYSPRQDYY GALHNQAHRV LGSQADPHGK
FALPPGVLEH FETATRDPAF FRLHKYMDNI FRKHKDSLTP YTKNELKFEG VNIDSIYEKG
NLETYFESFM YTGVNIMLLT NDVDDVDIAT YITDLAHKEL SFQEDVTNEG DIGVLETVRI
FAWPHIDDDH VEFSFNEGRW DVIEMDKFWV MLEHGHHSID RSSFDSTVTI PDRPSFHDIE
DRTSEAIPHG KELHIEEFES VTGLPNRFLI PKGLVKGKDM DVMVAVTSGE GLAAVEGLHR
SANFAHHGCP EVRYPDKRPH GYPLYRPVDD ERIITGVTNF KHIQVKVFHH
