ID   PHCY1_HOMAM             Reviewed;         684 AA.
AC   Q6KF82;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 46.
DE   RecName: Full=Pseudohemocyanin-1;
DE   Flags: Precursor; Fragment;
GN   Name=phc-1 {ECO:0000312|EMBL:CAB38042.1};
OS   Homarus americanus (American lobster).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC   Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Astacidea;
OC   Nephropoidea; Nephropidae; Homarus.
OX   NCBI_TaxID=6706;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:CAB38042.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 24-43, SUBUNIT, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Hemolymph {ECO:0000269|PubMed:10224079}, and
RC   Thorax {ECO:0000312|EMBL:CAB38042.1};
RX   PubMed=10224079; DOI=10.1074/jbc.274.19.13217;
RA   Burmester T.;
RT   "Identification, molecular cloning and phylogenetic analysis of a non-
RT   respiratory pseudo-hemocyanin of Homarus americanus.";
RL   J. Biol. Chem. 274:13217-13222(1999).
CC   -!- FUNCTION: Does not function as a hemocyanin.
CC       {ECO:0000269|PubMed:10224079}.
CC   -!- SUBUNIT: Hexamer. {ECO:0000269|PubMed:10224079}.
CC   -!- TISSUE SPECIFICITY: Strongly expressed in ovaries. Also expressed in
CC       heart. Not detected in hepatopancreas, gills, connective tissue or
CC       muscle. {ECO:0000269|PubMed:10224079}.
CC   -!- MISCELLANEOUS: Does not bind copper. {ECO:0000269|PubMed:10224079}.
CC   -!- SIMILARITY: Belongs to the tyrosinase family. Hemocyanin subfamily.
CC       {ECO:0000255}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJ132141; CAB38042.1; -; mRNA.
DR   AlphaFoldDB; Q6KF82; -.
DR   SMR; Q6KF82; -.
DR   PRIDE; Q6KF82; -.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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; PS00210; HEMOCYANIN_2; 1.
DR   PROSITE; PS00498; TYROSINASE_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycoprotein; Signal.
FT   SIGNAL          <1..23
FT                   /evidence="ECO:0000269|PubMed:10224079"
FT   CHAIN           24..684
FT                   /note="Pseudohemocyanin-1"
FT                   /id="PRO_0000234529"
FT   REGION          7..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        100
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        193
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        230
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        626
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   NON_TER         1
FT                   /evidence="ECO:0000312|EMBL:CAB38042.1"
SQ   SEQUENCE   684 AA;  79621 MW;  0B31A8DB6B1DC02D CRC64;
     SLVVAAAAAS PYSGSHDFSG FQRDEPDGVP TAQKQHDINF LLHKLYEPLH EANLKALEDS
     FDPLTHTANM PDAGVAVNKL MQEVKTQHLE ERHHWFSVFN ATQREEALLL VKVLLQCQDW
     PTAIGNAVYF RKMMNEETYV YALYTAIKHS PLTKHVVLPP LYEIMPHFFT SSEVIQQAYR
     AKMIGQPGKF NMNFTGTQNN PEHKIAYFGE DIGLSTHYIN WHIEYPFWWN ETFGYQIERR
     GENYFWVHHQ LVNRFEAERI SNHLQKIEKL HWERNLHEGF DPHTSYKNGE HFPFRHDDIH
     IEDVDKVAEV RDMIVMENRI RDAIAHGYVI DKEGNKVDIN NEHGIDILGE IIESCVYNPY
     NEYYGSLHNM GHMMLGHQGD PHAKYYDTPS VLEHYETTLR DPAFYKLHKY IDDLFRKHKD
     HLKPYSRKEL LFPGIAINNI HIDGPLETYF EDYEYSLMNA MDDKEEMKWE DNMEISAIIP
     RLRHKDFSFK VNIMNNNDEN KLATIRIFAW PHRDVNGVIM PFNEGRWHAI ELDKFWKYLA
     PGENEVTRKC DESSVTVPDV PSLKSLHEQA EAAIAGISEL NLEEFVSATG LPNRLLIPKG
     NAAGVEFKLV VAVTDGEADS VNDEINLTTK FHHYGHHGVY LDKKSHGYPL DRRVPDERLF
     HEIPNFGETI VKVFNHNEHV HRHE