HCY_SCYSE
ID HCY_SCYSE Reviewed; 650 AA.
AC C0HLU8;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 29-SEP-2021, sequence version 1.
DT 03-AUG-2022, entry version 4.
DE RecName: Full=Hemocyanin subunit {ECO:0000303|Ref.1};
OS Scylla serrata (Mud crab).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Brachyura;
OC Eubrachyura; Portunoidea; Portunidae; Scylla.
OX NCBI_TaxID=6761 {ECO:0000303|Ref.1};
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Hemolymph {ECO:0000269|Ref.1};
RA Prasanthi C., Ramesh B.K.;
RT "Characterization and molecular interactions of hemolymph proteins from two
RT mud crab species Scylla serrata (Forskal, 1775) and Scylla olivacea
RT (Herbst, 1796) from Visakhapatnam coast, Andhra Pradesh, India.";
RL Submitted (DEC-2020) to UniProtKB.
CC -!- FUNCTION: Hemocyanins are copper-containing oxygen carriers occurring
CC freely dissolved in the hemolymph of many mollusks and arthropods.
CC {ECO:0000250|UniProtKB:P84293}.
CC -!- SUBUNIT: Hexamer of a number of different chains.
CC {ECO:0000250|UniProtKB:P84293}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC {ECO:0000269|Ref.1}.
CC -!- TISSUE SPECIFICITY: Hemolymph. {ECO:0000269|Ref.1}.
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:0000250|UniProtKB:P84293}.
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:0000250|UniProtKB:P84293}.
CC -!- SIMILARITY: Belongs to the tyrosinase family. Hemocyanin subfamily.
CC {ECO:0000305}.
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DR SMR; C0HLU8; -.
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"
FT /id="PRO_0000453529"
FT BINDING 193
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:P04254"
FT BINDING 197
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:P04254"
FT BINDING 225
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:P04254"
FT BINDING 344
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:P04254"
FT BINDING 348
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:P04254"
FT BINDING 384
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:P04254"
FT CARBOHYD 120
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000250|UniProtKB:P84293"
FT CARBOHYD 172
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000250|UniProtKB:P84293"
FT CARBOHYD 309
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
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
