ID   SCAL2_STRCA             Reviewed;         142 AA.
AC   P83515;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2004, sequence version 1.
DT   25-MAY-2022, entry version 59.
DE   RecName: Full=Struthiocalcin-2;
DE            Short=SCA-2;
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, PHOSPHORYLATION AT SER-62; SER-66
RP   AND SER-68, 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=16834.1; Mass_error=2; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:14726203};
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DR   AlphaFoldDB; P83515; -.
DR   SMR; P83515; -.
DR   iPTMnet; P83515; -.
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; IPR016187; CTDL_fold.
DR   Pfam; PF00059; Lectin_C; 1.
DR   SMART; SM00034; CLECT; 1.
DR   SUPFAM; SSF56436; SSF56436; 1.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Extracellular matrix; Lectin;
KW   Phosphoprotein; Secreted.
FT   CHAIN           1..142
FT                   /note="Struthiocalcin-2"
FT                   /id="PRO_0000046721"
FT   DOMAIN          13..139
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT                   ECO:0000305"
FT   MOD_RES         62
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:14726203"
FT   MOD_RES         66
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:14726203"
FT   MOD_RES         68
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:14726203"
FT   DISULFID        6..17
FT                   /evidence="ECO:0000250|UniProtKB:Q9PRS8,
FT                   ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        34..138
FT                   /evidence="ECO:0000250|UniProtKB:Q9PRS8,
FT                   ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        113..130
FT                   /evidence="ECO:0000250|UniProtKB:Q9PRS8,
FT                   ECO:0000255|PROSITE-ProRule:PRU00040"
SQ   SEQUENCE   142 AA;  16601 MW;  AF9950BF166B8FF9 CRC64;
     RERAGCAKGW IPFDGRCYGF FPQELSWRRA EGFCQRLGAR THLASIHSEE EHQAIVSMLA
     SSQPYSDSEE EAGEEVWIGL HRPLGRRNWE WSDGTKLDYG SWYRDVFLRR RACVALEDTT
     DFATWDVELC SDRKPFICEY RT