CRC1_HOMGA
ID CRC1_HOMGA Reviewed; 181 AA.
AC P80029;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=Crustacyanin-C1 subunit;
OS Homarus gammarus (European lobster) (Homarus vulgaris).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Astacidea;
OC Nephropoidea; Nephropidae; Homarus.
OX NCBI_TaxID=6707;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=1935978; DOI=10.1111/j.1432-1033.1991.tb16340.x;
RA Keen J.N., Caceres I., Eliopoulos E.E., Zagalsky P.F., Findlay J.B.C.;
RT "Complete sequence and model for the C1 subunit of the carotenoprotein,
RT crustacyanin, and model for the dimer, beta-crustacyanin, formed from the
RT C1 and A2 subunits with astaxanthin.";
RL Eur. J. Biochem. 202:31-40(1991).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS) OF HOMODIMER.
RX PubMed=11526314; DOI=10.1107/s0907444901009362;
RA Gordon E.J., Leonard G.A., McSweeney S., Zagalsky P.F.;
RT "The C1 subunit of alpha-crustacyanin: the de novo phasing of the crystal
RT structure of a 40 kDa homodimeric protein using the anomalous scattering
RT from S atoms combined with direct methods.";
RL Acta Crystallogr. D 57:1230-1237(2001).
CC -!- FUNCTION: Binds the carotenoid astaxanthin (AXT) which provides the
CC blue coloration to the carapace of the lobster.
CC -!- SUBUNIT: Oligomer; Can form dimers (beta-crustacyanin); or complexes of
CC 16 subunits (alpha-crustacyanin). There are five types of subunits: A1,
CC A2, A3, C1 and C2.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC -!- TISSUE SPECIFICITY: Found in the carapace.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Squeeze me - Issue 26 of
CC September 2002;
CC URL="https://web.expasy.org/spotlight/back_issues/026";
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DR PIR; S19534; S19534.
DR PDB; 1H91; X-ray; 1.40 A; A/B=2-180.
DR PDB; 1I4U; X-ray; 1.15 A; A/B=1-181.
DR PDB; 1OBQ; X-ray; 1.85 A; A/B=1-181.
DR PDB; 1OBU; X-ray; 2.00 A; A/B=1-181.
DR PDB; 1S2P; X-ray; 1.30 A; A/B=1-181.
DR PDB; 4ALO; X-ray; 2.37 A; A/B=1-180.
DR PDBsum; 1H91; -.
DR PDBsum; 1I4U; -.
DR PDBsum; 1OBQ; -.
DR PDBsum; 1OBU; -.
DR PDBsum; 1S2P; -.
DR PDBsum; 4ALO; -.
DR AlphaFoldDB; P80029; -.
DR SMR; P80029; -.
DR EvolutionaryTrace; P80029; -.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0031409; F:pigment binding; IEA:UniProtKB-KW.
DR Gene3D; 2.40.128.20; -; 1.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR003057; Invtbrt_color.
DR InterPro; IPR022271; Lipocalin_ApoD.
DR InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
DR Pfam; PF00061; Lipocalin; 1.
DR PIRSF; PIRSF036893; Lipocalin_ApoD; 1.
DR PRINTS; PR01273; INVTBRTCOLOR.
DR SUPFAM; SSF50814; SSF50814; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Pigment; Secreted;
KW Transport.
FT CHAIN 1..181
FT /note="Crustacyanin-C1 subunit"
FT /id="PRO_0000201011"
FT DISULFID 12..121
FT DISULFID 51..173
FT DISULFID 117..150
FT STRAND 7..10
FT /evidence="ECO:0007829|PDB:1I4U"
FT HELIX 17..24
FT /evidence="ECO:0007829|PDB:1I4U"
FT HELIX 25..27
FT /evidence="ECO:0007829|PDB:1I4U"
FT HELIX 28..31
FT /evidence="ECO:0007829|PDB:1I4U"
FT STRAND 33..41
FT /evidence="ECO:0007829|PDB:1I4U"
FT STRAND 48..58
FT /evidence="ECO:0007829|PDB:1I4U"
FT STRAND 63..71
FT /evidence="ECO:0007829|PDB:1I4U"
FT STRAND 76..85
FT /evidence="ECO:0007829|PDB:1I4U"
FT STRAND 91..97
FT /evidence="ECO:0007829|PDB:1I4U"
FT STRAND 102..110
FT /evidence="ECO:0007829|PDB:1I4U"
FT STRAND 112..123
FT /evidence="ECO:0007829|PDB:1I4U"
FT STRAND 127..141
FT /evidence="ECO:0007829|PDB:1I4U"
FT HELIX 144..156
FT /evidence="ECO:0007829|PDB:1I4U"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:1I4U"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:1I4U"
FT HELIX 175..178
FT /evidence="ECO:0007829|PDB:1I4U"
SQ SEQUENCE 181 AA; 20667 MW; 6A05C7CBA3498EE8 CRC64;
DKIPDFVVPG KCASVDRNKL WAEQTPNRNS YAGVWYQFAL TNNPYQLIEK CVRNEYSFDG
KQFVIKSTGI AYDGNLLKRN GKLYPNPFGE PHLSIDYENS FAAPLVILET DYSNYACLYS
CIDYNFGYHS DFSFIFSRSA NLADQYVKKC EAAFKNINVD TTRFVKTVQG SSCPYDTQKT
L