ID Q5G2A5_METMG Unreviewed; 675 AA.
AC Q5G2A5;
DT 01-MAR-2005, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2005, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Hemocyanin subunit 4 {ECO:0000313|EMBL:AAW57892.1};
GN Name=Hc4 {ECO:0000313|EMBL:AAW57892.1};
OS Metacarcinus magister (Dungeness crab) (Cancer magister).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Brachyura;
OC Eubrachyura; Cancroidea; Cancridae; Metacarcinus.
OX NCBI_TaxID=29965 {ECO:0000313|EMBL:AAW57892.1};
RN [1] {ECO:0000313|EMBL:AAW57892.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Hepatopancreas {ECO:0000313|EMBL:AAW57892.1};
RX PubMed=16501063;
RA Terwilliger N.B., Ryan M.C.;
RT "Functional and phylogenetic analyses of phenoloxidases from brachyuran
RT (Cancer magister) and branchiopod (Artemia franciscana, Triops
RT longicaudatus) crustaceans.";
RL Biol. Bull. 210:38-50(2006).
CC -!- SIMILARITY: Belongs to the tyrosinase family. Hemocyanin subfamily.
CC {ECO:0000256|ARBA:ARBA00009470}.
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DR EMBL; AY861679; AAW57892.1; -; mRNA.
DR AlphaFoldDB; Q5G2A5; -.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 1.10.1280.10; Di-copper center containing domain from catechol oxidase; 1.
DR Gene3D; 2.60.40.1520; Hemocyanin, C-terminal domain; 1.
DR Gene3D; 1.20.1370.10; Hemocyanin, N-terminal domain; 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:SF5; FAT-BODY PROTEIN 1-RELATED; 1.
DR PANTHER; PTHR11511; LARVAL STORAGE PROTEIN/PHENOLOXIDASE; 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; SSF48056; Di-copper centre-containing domain; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF48050; Hemocyanin, N-terminal domain; 1.
DR PROSITE; PS00209; HEMOCYANIN_1; 1.
DR PROSITE; PS00210; HEMOCYANIN_2; 1.
DR PROSITE; PS00498; TYROSINASE_2; 1.
PE 2: Evidence at transcript level;
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..675
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012407061"
FT DOMAIN 399..410
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00498"
SQ SEQUENCE 675 AA; 77093 MW; 3566FF8F34332528 CRC64;
MKLLVLFALV AAAVAWPSFG MMADSAGAPD AHKQHDVNSV LWKVYEDIRD PHLKELSQSF
DPLSGHYDDD GVAAKRLMKE LNENRLLEQN HWFSLFNTRQ RKEALMLYDV LEHSTDWSTF
AGNAAFFRVH MNEGEFVYAL YAAVIHSELT QHVVLPPLYE VTPHLFTNSE VIQEAYKAKM
TQTAAKIESH FTGSKSNPEQ RVAYFGEDIG MNTHHVTWHL EFPFWWDDAH ENHHIERKGE
SFFWVHHQLT VRFDAERLSN YLDPVDELHW DDVIHEGFAP HTMYKYGGYF PSRPDNVHFE
DVDGVARVRD MLILESRIRD AIAHGYVTGR DGSIISISDS HGIDVLGDVI ESSLYSPNPE
YYGALHNTAH MMLGRQGDPH GKFDLPPGVL EHFETATRDP AFFRLHKYMD NIFREHKDSL
TPYTKDELEF PGIEIDSFSL SNRLETYFED FEYSLINAVD DTAEIADVPI STVVKRLTHK
SFTAKCVINN NNEHDVIATV RIFAWPKYDN NHVEFSFNDG RWNAIEMDKY WTKLTPGPNT
ITRSSMDSSV TVPDVPSFLT LIEKTEEAVS SGSELHLEDY VSGLGLPNRF LLSKGTTKGM
DFHLVVFVSD GAKDAAIDGL LENTSFNHYG AHSGKYPDKQ PHGYPLDRRV DDKRIITGVT
NFKGMDVKVY HVEEQ
//
