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   27-MAR-2024, entry version 113.
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:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0031409; F:pigment binding; IEA:UniProtKB-KW.
DR   GO; GO:0006950; P:response to stress; IEA:UniProt.
DR   CDD; cd19436; lipocalin_crustacyanin; 1.
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   PANTHER; PTHR10612; APOLIPOPROTEIN D; 1.
DR   PANTHER; PTHR10612:SF34; APOLIPOPROTEIN D; 1.
DR   Pfam; PF00061; Lipocalin; 1.
DR   PIRSF; PIRSF036893; Lipocalin_ApoD; 1.
DR   PRINTS; PR01273; INVTBRTCOLOR.
DR   PRINTS; PR00179; LIPOCALIN.
DR   SUPFAM; SSF50814; Lipocalins; 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
//