ID   CRA1_HOMGA              Reviewed;         181 AA.
AC   P58989;
DT   13-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-2002, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Crustacyanin-A1 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   X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS) OF HOMODIMER.
RX   PubMed=11526313; DOI=10.1107/s0907444901009350;
RA   Cianci M., Rizkallah P.J., Olczak A., Raftery J., Chayen N.E.,
RA   Zagalsky P.F., Helliwell J.R.;
RT   "Structure of lobster apocrustacyanin A1 using softer X-rays.";
RL   Acta Crystallogr. D 57:1219-1229(2001).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF HETERODIMER OF A1 AND A3 IN
RP   COMPLEX WITH ASTAXANTHIN.
RX   PubMed=12119396; DOI=10.1073/pnas.152088999;
RA   Cianci M., Rizkallah P.J., Olczak A., Raftery J., Chayen N.E.,
RA   Zagalsky P.F., Helliwell J.R.;
RT   "The molecular basis of the coloration mechanism in lobster shell: beta-
RT   crustacyanin at 3.2-A resolution.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:9795-9800(2002).
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. {ECO:0000269|PubMed:12119396}.
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   PDB; 1GKA; X-ray; 3.23 A; A=2-181.
DR   PDB; 1S44; X-ray; 1.60 A; A/B=2-181.
DR   PDBsum; 1GKA; -.
DR   PDBsum; 1S44; -.
DR   AlphaFoldDB; P58989; -.
DR   SMR; P58989; -.
DR   MINT; P58989; -.
DR   EvolutionaryTrace; P58989; -.
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; Chromophore; Disulfide bond; Pigment; Secreted; Transport.
FT   CHAIN           1..181
FT                   /note="Crustacyanin-A1 subunit"
FT                   /id="PRO_0000201009"
FT   DISULFID        12..121
FT   DISULFID        51..173
FT   DISULFID        117..150
FT   STRAND          7..11
FT                   /evidence="ECO:0007829|PDB:1S44"
FT   HELIX           17..24
FT                   /evidence="ECO:0007829|PDB:1S44"
FT   HELIX           25..27
FT                   /evidence="ECO:0007829|PDB:1S44"
FT   HELIX           28..31
FT                   /evidence="ECO:0007829|PDB:1S44"
FT   STRAND          33..41
FT                   /evidence="ECO:0007829|PDB:1S44"
FT   STRAND          48..58
FT                   /evidence="ECO:0007829|PDB:1S44"
FT   STRAND          63..71
FT                   /evidence="ECO:0007829|PDB:1S44"
FT   STRAND          74..85
FT                   /evidence="ECO:0007829|PDB:1S44"
FT   STRAND          91..97
FT                   /evidence="ECO:0007829|PDB:1S44"
FT   STRAND          98..100
FT                   /evidence="ECO:0007829|PDB:1GKA"
FT   STRAND          102..110
FT                   /evidence="ECO:0007829|PDB:1S44"
FT   STRAND          112..123
FT                   /evidence="ECO:0007829|PDB:1S44"
FT   STRAND          127..141
FT                   /evidence="ECO:0007829|PDB:1S44"
FT   HELIX           144..156
FT                   /evidence="ECO:0007829|PDB:1S44"
FT   HELIX           161..163
FT                   /evidence="ECO:0007829|PDB:1S44"
FT   STRAND          164..166
FT                   /evidence="ECO:0007829|PDB:1S44"
FT   STRAND          170..173
FT                   /evidence="ECO:0007829|PDB:1GKA"
FT   HELIX           175..178
FT                   /evidence="ECO:0007829|PDB:1S44"
SQ   SEQUENCE   181 AA;  20652 MW;  285EADC1A4F2E353 CRC64;
     DKIPNFVVPG KCASVDRNKL WAEQTPNRNS YAGVWYQFAL TNNPYQLIEK CVRNEYSFDG
     KQFVIKSTGI AYDGNLLKRN GKLYPNPFGE PHLSIDYENS FAAPLVILET DYSNYACLYS
     CIDYNFGYHS DFSFIFSRSA NLADQYVKKC EAAFKNINVD TTRFVKTVQG SSCPYDTQKT
     V