OC17_CHICK
ID OC17_CHICK Reviewed; 142 AA.
AC Q9PRS8;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2003, sequence version 2.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Ovocleidin-17;
DE Short=OC-17;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, MASS SPECTROMETRY, DISULFIDE BONDS, AND PHOSPHORYLATION
RP AT SER-61 AND SER-67.
RC TISSUE=Eggshell matrix {ECO:0000269|PubMed:10410246};
RX PubMed=10410246; DOI=10.1080/15216549900202123;
RA Mann K., Siedler F.;
RT "The amino acid sequence of ovocleidin 17, a major protein of the avian
RT eggshell calcified layer.";
RL Biochem. Mol. Biol. Int. 47:997-1007(1999).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 1-24, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Eggshell matrix {ECO:0000269|PubMed:7648490};
RX PubMed=7648490; DOI=10.1007/bf00298593;
RA Hincke M.T., Tsang C.P.W., Courtney M., Hill V., Narbaitz R.;
RT "Purification and immunochemistry of a soluble matrix protein of the
RT chicken eggshell (ovocleidin 17).";
RL Calcif. Tissue Int. 56:578-583(1995).
RN [3] {ECO:0000305}
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
RX PubMed=12144522; DOI=10.2174/0929866023408805;
RA Reyes-Grajeda J.P., Jauregui-Zuniga D., Rodriguez-Romero A.,
RA Hernandez-Santoyo A., Bolanos-Garcia V.M., Moreno A.;
RT "Crystallization and preliminary X-ray analysis of ovocleidin-17 a major
RT protein of the Gallus gallus eggshell calcified layer.";
RL Protein Pept. Lett. 9:253-257(2002).
CC -!- FUNCTION: May form proteinaceous networks during the construction of
CC the eggshell which then may control the deposition of the mineral
CC phase. {ECO:0000303|PubMed:10410246}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000269|PubMed:7648490}. Note=Eggshell matrix. Mostly in
CC the mammillary bodies.
CC -!- TISSUE SPECIFICITY: Expressed in the shell gland mucosa. Not detected
CC in hen liver, magnum, isthmus, cartilage, bone or in egg white or yolk.
CC {ECO:0000269|PubMed:7648490}.
CC -!- MASS SPECTROMETRY: Mass=15453.8; Mass_error=2; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:10410246};
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DR PDB; 1GZ2; X-ray; 1.50 A; A=1-142.
DR PDBsum; 1GZ2; -.
DR AlphaFoldDB; Q9PRS8; -.
DR SMR; Q9PRS8; -.
DR iPTMnet; Q9PRS8; -.
DR VEuPathDB; HostDB:LOC121109246; -.
DR PhylomeDB; Q9PRS8; -.
DR EvolutionaryTrace; Q9PRS8; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0031012; C:extracellular matrix; IDA:AgBase.
DR GO; GO:0005576; C:extracellular region; IDA:AgBase.
DR GO; GO:0005615; C:extracellular space; IDA:AgBase.
DR GO; GO:1990377; C:organomineral extracellular matrix; IDA:AgBase.
DR GO; GO:0003823; F:antigen binding; IDA:AgBase.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:1990430; F:extracellular matrix protein binding; IPI:AgBase.
DR GO; GO:0043167; F:ion binding; TAS:AgBase.
DR GO; GO:0001530; F:lipopolysaccharide binding; IDA:AgBase.
DR GO; GO:0042834; F:peptidoglycan binding; IDA:AgBase.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0019731; P:antibacterial humoral response; IDA:AgBase.
DR GO; GO:0019730; P:antimicrobial humoral response; IDA:AgBase.
DR GO; GO:0031214; P:biomineral tissue development; IDA:AgBase.
DR GO; GO:0031215; P:shell calcification; TAS:AgBase.
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 3D-structure; Direct protein sequencing; Disulfide bond;
KW Extracellular matrix; Glycoprotein; Lectin; Phosphoprotein;
KW Reference proteome; Secreted.
FT CHAIN 1..142
FT /note="Ovocleidin-17"
FT /id="PRO_0000046687"
FT DOMAIN 12..139
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT MOD_RES 61
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:10410246"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:10410246"
FT CARBOHYD 59
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 5..16
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:10410246"
FT DISULFID 33..138
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:10410246"
FT DISULFID 113..130
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:10410246"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:1GZ2"
FT STRAND 15..24
FT /evidence="ECO:0007829|PDB:1GZ2"
FT HELIX 26..34
FT /evidence="ECO:0007829|PDB:1GZ2"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:1GZ2"
FT HELIX 48..59
FT /evidence="ECO:0007829|PDB:1GZ2"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:1GZ2"
FT STRAND 75..80
FT /evidence="ECO:0007829|PDB:1GZ2"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:1GZ2"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:1GZ2"
FT STRAND 112..116
FT /evidence="ECO:0007829|PDB:1GZ2"
FT TURN 118..121
FT /evidence="ECO:0007829|PDB:1GZ2"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:1GZ2"
FT STRAND 134..141
FT /evidence="ECO:0007829|PDB:1GZ2"
SQ SEQUENCE 142 AA; 15300 MW; A1E8FAF1A1655F78 CRC64;
DPDGCGPGWV PTPGGCLGFF SRELSWSRAE SFCRRWGPGS HLAAVRSAAE LRLLAELLNA
SRGGDGSGEG ADGRVWIGLH RPAGSRSWRW SDGTAPRFAS WHRTAKARRG GRCAALRDEE
AFTSWAARPC TERNAFVCKA AA
