ID   DCAL2_DRONO             Reviewed;         142 AA.
AC   P84616;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 2.
DT   25-MAY-2022, entry version 51.
DE   RecName: Full=Dromaiocalcin-2;
DE            Short=DCA-2;
OS   Dromaius novaehollandiae (Emu).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Palaeognathae; Casuariiformes; Dromaiidae; Dromaius.
OX   NCBI_TaxID=8790;
RN   [1]
RP   PROTEIN SEQUENCE, MASS SPECTROMETRY, AND PHOSPHORYLATION AT SER-62 AND
RP   SER-68.
RC   TISSUE=Eggshell matrix;
RX   PubMed=16403478; DOI=10.1016/j.cbpb.2005.11.003;
RA   Mann K., Siedler F.;
RT   "Amino acid sequences and phosphorylation sites of emu and rhea eggshell C-
RT   type lectin-like proteins.";
RL   Comp. Biochem. Physiol. 143B:160-170(2006).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 1-30.
RC   TISSUE=Eggshell matrix {ECO:0000269|PubMed:15484722};
RX   PubMed=15484722; DOI=10.1080/00071660400001157;
RA   Mann K.;
RT   "Identification of the major proteins of the organic matrix of emu
RT   (Dromaius novaehollandiae) and rhea (Rhea americana) eggshell calcified
RT   layer.";
RL   Br. Poult. Sci. 45:483-490(2004).
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix. Note=Eggshell matrix.
CC   -!- PTM: A minor form with some unmodified Ser-68 and partial
CC       phosphorylation of Ser-66 may also occur.
CC       {ECO:0000269|PubMed:16403478}.
CC   -!- MASS SPECTROMETRY: Mass=16645.6; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:16403478};
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DR   AlphaFoldDB; P84616; -.
DR   SMR; P84616; -.
DR   iPTMnet; P84616; -.
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="Dromaiocalcin-2"
FT                   /id="PRO_0000046717"
FT   DOMAIN          13..139
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   MOD_RES         62
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:16403478"
FT   MOD_RES         68
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:16403478"
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;  16490 MW;  60B567C659F53E55 CRC64;
     EEEIGCTSGW VPFDGRCYGF FPQELSWRRA ESFCQRLGAR THLVSIHNEE EHQAIISMLA
     SSQPYSDSEE QEANGDVWIG LRLSLRRLWE WSDGTKLDYG SWYRDVLPRR RACAALEDTA
     DFASWDVELC SDRKPFICAY RT