ID   SCAL1_STRCA             Reviewed;         132 AA.
AC   P83514;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2004, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=Struthiocalcin-1;
DE            Short=SCA-1;
OS   Struthio camelus (Common ostrich).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Palaeognathae; Struthioniformes; Struthionidae;
OC   Struthio.
OX   NCBI_TaxID=8801 {ECO:0000305};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC   TISSUE=Eggshell matrix {ECO:0000269|PubMed:14726203};
RX   PubMed=14726203; DOI=10.1016/j.bbapap.2003.09.006;
RA   Mann K., Siedler F.;
RT   "Ostrich (Struthio camelus) eggshell matrix contains two different C-type
RT   lectin-like proteins. Isolation, amino acid sequence, and posttranslational
RT   modifications.";
RL   Biochim. Biophys. Acta 1696:41-50(2004).
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000269|PubMed:14726203}. Note=Eggshell matrix.
CC   -!- MASS SPECTROMETRY: Mass=15343.2; Mass_error=4; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:14726203};
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DR   PDB; 4UWW; X-ray; 1.44 A; A=1-132.
DR   PDB; 4UXM; X-ray; 1.50 A; A=1-132.
DR   PDBsum; 4UWW; -.
DR   PDBsum; 4UXM; -.
DR   AlphaFoldDB; P83514; -.
DR   SMR; P83514; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.100.10; -; 1.
DR   InterPro; IPR001304; C-type_lectin-like.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR018378; C-type_lectin_CS.
DR   InterPro; IPR016187; CTDL_fold.
DR   Pfam; PF00059; Lectin_C; 1.
DR   SMART; SM00034; CLECT; 1.
DR   SUPFAM; SSF56436; SSF56436; 1.
DR   PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disulfide bond;
KW   Extracellular matrix; Lectin; Secreted.
FT   CHAIN           1..132
FT                   /note="Struthiocalcin-1"
FT                   /id="PRO_0000046720"
FT   DOMAIN          10..129
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT                   ECO:0000305"
FT   DISULFID        3..14
FT                   /evidence="ECO:0000250|UniProtKB:Q9PRS8,
FT                   ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        31..128
FT                   /evidence="ECO:0000250|UniProtKB:Q9PRS8,
FT                   ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        103..120
FT                   /evidence="ECO:0000250|UniProtKB:Q9PRS8,
FT                   ECO:0000255|PROSITE-ProRule:PRU00040"
FT   STRAND          8..10
FT                   /evidence="ECO:0007829|PDB:4UWW"
FT   STRAND          13..22
FT                   /evidence="ECO:0007829|PDB:4UWW"
FT   HELIX           24..34
FT                   /evidence="ECO:0007829|PDB:4UWW"
FT   HELIX           46..57
FT                   /evidence="ECO:0007829|PDB:4UWW"
FT   HELIX           59..62
FT                   /evidence="ECO:0007829|PDB:4UWW"
FT   STRAND          68..75
FT                   /evidence="ECO:0007829|PDB:4UWW"
FT   STRAND          78..81
FT                   /evidence="ECO:0007829|PDB:4UWW"
FT   TURN            98..100
FT                   /evidence="ECO:0007829|PDB:4UWW"
FT   STRAND          103..106
FT                   /evidence="ECO:0007829|PDB:4UWW"
FT   HELIX           108..110
FT                   /evidence="ECO:0007829|PDB:4UWW"
FT   STRAND          114..118
FT                   /evidence="ECO:0007829|PDB:4UWW"
FT   STRAND          124..131
FT                   /evidence="ECO:0007829|PDB:4UWW"
SQ   SEQUENCE   132 AA;  15353 MW;  F7BD1DF2990B2945 CRC64;
     DKCPKGWLDF RGNCYGYFRY ELPWKRAEAW CRSIRAGAHL ASIHTSEEHR AIAKFISQYH
     HGEEEEDVWI GLFRWNSVWA WIDGSKKHYS ALDDDDYPKG KHCAVLDESS GFLSWDNDSC
     GERNAFICKC TA