PHCY2_HOMAM
ID PHCY2_HOMAM Reviewed; 681 AA.
AC Q6KF81;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 45.
DE RecName: Full=Pseudohemocyanin-2;
DE Flags: Precursor; Fragment;
GN Name=phc-2 {ECO:0000312|EMBL:CAB38043.1};
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:CAB38043.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 22-33, SUBUNIT, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Hemolymph {ECO:0000269|PubMed:10224079}, and
RC Thorax {ECO:0000312|EMBL:CAB38043.1};
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}.
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DR EMBL; AJ132142; CAB38043.1; -; mRNA.
DR AlphaFoldDB; Q6KF81; -.
DR SMR; Q6KF81; -.
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..21
FT /evidence="ECO:0000269|PubMed:10224079"
FT CHAIN 22..681
FT /note="Pseudohemocyanin-2"
FT /id="PRO_0000234530"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 191
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 624
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT NON_TER 1
FT /evidence="ECO:0000312|EMBL:CAB38043.1"
SQ SEQUENCE 681 AA; 79222 MW; 44323B74A0C21E69 CRC64;
VLLCSLVAAT AAWPYFGGFQ RDEPDGVPTA QKQHDINFLL HKLYEPLHEA NLKALEDSFD
PLAHTANMPD GGVAVNKLMQ EVKTQHLEER HHWFSVFNAT QREEALLLVK VLLQCQDWPT
AIGNAVYFRK MMNEETYVYA LYTAIKHSPL TKHVVLPPLY EIMPHFFTSS EVIQQAYRAK
LIEKPGRFNM NFTGTQNNPE HKIAYFGEDI GLSTHYINWH IEYPFWWNET FGYQIERRGE
NYFWVHHQLV NRFEAERISN HLQKIEKLHW ERNLHEGFDP HTSYKNGNPF PFRHDDIHIE
DVDKVAEVRD MIVMENRIRD AIAHGYVIDK EGNKVDINNE HGIDILGDII ESCVYNPYNE
YYGSLHNMGH MMLGHQGDPH AKYYDTPSVL EHYETALRDP AFYKLHKYID DLFRKHKDHL
KPYSQEDLLF PGVAVNMIDI DGPLETYFED YEYSLMNAMD DKEEMIWEDS MEISAIIPRL
RHKDFSFKVN IMNNNDENKL STIRIFAWPH RDVNGVIMPF NEGRWHAIEL DKFQKELIPG
ENTITRKSSE SSVTVPDVPS LKSLHEQTEA AIAGSSELNL DEFVSATGLP NRLLIPKGNE
AGVEFKLVVA VTDGVADSVN DEINLTTKFH HYGHHGVYLD KKPHGYPLDR RVPDERLFHE
IPNFGETIVK VFNRDEHVYH H