OC116_CHICK
ID OC116_CHICK Reviewed; 743 AA.
AC F1NSM7; Q9PUT1;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Ovocleidin-116 {ECO:0000312|EMBL:AAF00982.3};
DE Short=OC-116 {ECO:0000303|PubMed:20665709};
DE Flags: Precursor;
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, ECO:0000312|EMBL:AAF00982.3}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 19-40; 589-611 AND 617-628,
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RC STRAIN=Isa brown {ECO:0000269|PubMed:10551857}, and
RC White leghorn {ECO:0000269|PubMed:10551857};
RC TISSUE=Eggshell matrix {ECO:0000312|EMBL:AAF00982.3}, and
RC Uterus {ECO:0000269|PubMed:10551857};
RX PubMed=10551857; DOI=10.1074/jbc.274.46.32915;
RA Hincke M.T., Gautron J., Tsang C.P., McKee M.D., Nys Y.;
RT "Molecular cloning and ultrastructural localization of the core protein of
RT an eggshell matrix proteoglycan, ovocleidin-116.";
RL J. Biol. Chem. 274:32915-32923(1999).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAF00982.3}
RP SEQUENCE REVISION, PROTEIN SEQUENCE OF 19-38; 122-133; 234-245; 253-267;
RP 286-300; 390-409; 459-478; 530-549; 589-598; 644-655; 657-668; 660-669 AND
RP 687-706, FUNCTION, GLYCOSYLATION AT ASN-62 AND ASN-293, AND DISULFIDE BOND.
RC TISSUE=Eggshell matrix {ECO:0000312|EMBL:AAF00982.3};
RX PubMed=12225802; DOI=10.1016/s0945-053x(02)00031-8;
RA Mann K., Hincke M.T., Nys Y.;
RT "Isolation of ovocleidin-116 from chicken eggshells, correction of its
RT amino acid sequence and identification of disulfide bonds and glycosylated
RT Asn.";
RL Matrix Biol. 21:383-387(2002).
RN [3] {ECO:0000312|Ensembl:ENSGALP00000017755}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15592404; DOI=10.1038/nature03154;
RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA Wilson R.K.;
RT "Sequence and comparative analysis of the chicken genome provide unique
RT perspectives on vertebrate evolution.";
RL Nature 432:695-716(2004).
RN [4] {ECO:0000305}
RP TISSUE SPECIFICITY.
RX PubMed=18648057; DOI=10.3382/ps.2008-00031;
RA Horvat-Gordon M., Yu F., Burns D., Leach R.M. Jr.;
RT "Ovocleidin (OC 116) is present in avian skeletal tissues.";
RL Poult. Sci. 87:1618-1623(2008).
RN [5] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=20665709; DOI=10.1002/jez.b.21366;
RA Bardet C., Vincent C., Lajarille M.C., Jaffredo T., Sire J.Y.;
RT "OC-116, the chicken ortholog of mammalian MEPE found in eggshell, is also
RT expressed in bone cells.";
RL J. Exp. Zool. B Mol. Dev. Evol. 314:653-662(2010).
CC -!- FUNCTION: Major component of the eggshell matrix. May play an important
CC role in the regulation of calcite growth during eggshell calcification.
CC May also regulate the mineralization process in developing and growing
CC bones. {ECO:0000269|PubMed:12225802, ECO:0000303|PubMed:10551857,
CC ECO:0000303|PubMed:20665709}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000269|PubMed:10551857}. Note=Synthesized and secreted by
CC the granular epithelial cells of the uterus and incorporated into the
CC eggshell matrix. {ECO:0000269|PubMed:10551857}.
CC -!- TISSUE SPECIFICITY: In the eggshell, expressed mainly in the palisade
CC and mammillary layers. Expression also detected in the hypertrophic
CC zone of the epiphyseal growth plate, and in cortical and medullary bone
CC (at protein level). Highly expressed in uterus. Not detected in the
CC proximal oviduct, liver, magnum, duodenum and kidney.
CC {ECO:0000269|PubMed:10551857, ECO:0000269|PubMed:18648057,
CC ECO:0000269|PubMed:20665709}.
CC -!- DEVELOPMENTAL STAGE: Expressed at high levels at the middle of the
CC calcification stage of shell formation. Expression levels are similar
CC at 3-4 hours post-oviposition prior to entry of the egg into the uterus
CC and at 16-17 hours post-oviposition during eggshell calcification.
CC Expressed in tibia from E5 and in mandible from E7 until the end of
CC embryonic development at E19. Expression detected first in osteoblasts,
CC in later stages both in osteoblasts and osteocytes, and by the end of
CC embryonic development mainly in osteocytes.
CC {ECO:0000269|PubMed:10551857, ECO:0000269|PubMed:20665709}.
CC -!- PTM: Asn-62 is fully glycosylated, whereas only less than 10% of Asn-
CC 293 seem to be glycosylated. {ECO:0000269|PubMed:12225802}.
CC -!- SIMILARITY: Belongs to the osteoregulin family. {ECO:0000255}.
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DR EMBL; AF148716; AAF00982.3; -; mRNA.
DR EMBL; AADN02009016; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_989900.1; NM_204569.1.
DR AlphaFoldDB; F1NSM7; -.
DR STRING; 9031.ENSGALP00000017755; -.
DR iPTMnet; F1NSM7; -.
DR PaxDb; F1NSM7; -.
DR Ensembl; ENSGALT00000017776; ENSGALP00000017755; ENSGALG00000010927.
DR GeneID; 395256; -.
DR KEGG; gga:395256; -.
DR CTD; 56955; -.
DR VEuPathDB; HostDB:geneid_395256; -.
DR eggNOG; ENOG502SW2S; Eukaryota.
DR GeneTree; ENSGT00390000010702; -.
DR HOGENOM; CLU_022074_0_0_1; -.
DR InParanoid; F1NSM7; -.
DR OMA; CNTKHGF; -.
DR Reactome; R-GGA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-GGA-8957275; Post-translational protein phosphorylation.
DR PRO; PR:F1NSM7; -.
DR Proteomes; UP000000539; Chromosome 4.
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:0030141; C:secretory granule; IDA:AgBase.
DR GO; GO:1990430; F:extracellular matrix protein binding; IPI:AgBase.
DR GO; GO:0031214; P:biomineral tissue development; IBA:GO_Central.
DR GO; GO:0031215; P:shell calcification; IEP:AgBase.
DR InterPro; IPR009837; MEPE.
DR PANTHER; PTHR16510; PTHR16510; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Extracellular matrix;
KW Glycoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:10551857,
FT ECO:0000269|PubMed:12225802"
FT CHAIN 19..743
FT /note="Ovocleidin-116"
FT /evidence="ECO:0000269|PubMed:10551857,
FT ECO:0000269|PubMed:12225802"
FT /id="PRO_0000411994"
FT REGION 68..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 333..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 505..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 549..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 628..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 692..743
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..437
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 706..720
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 721..735
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12225802"
FT CARBOHYD 293
FT /note="N-linked (GlcNAc...) asparagine; partial"
FT /evidence="ECO:0000269|PubMed:12225802"
FT DISULFID 31..42
FT /evidence="ECO:0000269|PubMed:12225802"
FT CONFLICT 94
FT /note="A -> V (in Ref. 1; AAF00982)"
FT /evidence="ECO:0000305"
FT CONFLICT 108
FT /note="T -> P (in Ref. 1; AAF00982)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="Q -> H (in Ref. 1; AAF00982)"
FT /evidence="ECO:0000305"
FT CONFLICT 197
FT /note="E -> K (in Ref. 1; AAF00982)"
FT /evidence="ECO:0000305"
FT CONFLICT 208
FT /note="P -> T (in Ref. 1; AAF00982)"
FT /evidence="ECO:0000305"
FT CONFLICT 438
FT /note="S -> T (in Ref. 1; AAF00982)"
FT /evidence="ECO:0000305"
FT CONFLICT 457
FT /note="A -> S (in Ref. 1; AAF00982)"
FT /evidence="ECO:0000305"
FT CONFLICT 490
FT /note="A -> S (in Ref. 1; AAF00982)"
FT /evidence="ECO:0000305"
FT CONFLICT 727
FT /note="H -> R (in Ref. 1; AAF00982)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 743 AA; 76870 MW; 04F012A6D0E9D046 CRC64;
MRATLFCLCL CLLGTVLPTP VSLPARARGN CPGQHQILLK GCNTKHGFYI FQYIYSHLMQ
KNQTQVKKEE GDHQGTIHGH WLGKVDGEAP GQGAGSSHVP EDKDSPKTHS HITPASKGEG
RALRPGIGDS NSVYPTSTSV EGSGDMGSIL LGEIINGEDG LPQSTHPGGP HGDGDGGNGV
LVDGAVTAGR ERASGSEGAG SEGGSHAPVP DQGQAGTMGT GDSAITSVTD SAITSVTKKE
DVHVDTEGID EFAYIPDVDA VTITRGQDGE THISPEDEVK IFIGRANIQV GENDSSVGSA
GATSEANVIP TVVTVRPQGH PEESATMATL HHGDSVTSRP VGHPSVGNSG DGATEIHSGQ
ELEAPSPWES TGGDATVTMA VGVQSGKGRS GQRALGKHSL PATMTTRGGR GTASSGLTTG
DCSTAASTPS RKGSHVVSAG QGESGEVGTA GPERQRARVQ QEVAPARGVV GGMVVPEGHR
ARVQQEVAPA RGVVGGMVVP EGHRARTQPE VASAPSTVGK AAPERHRNRA QQEVAPVPSM
VVETVAPERH RARVRPESAR LGQAARPEVA PAPSTGGRIV APGGHRARVW PGAAPAPGVV
GVARPAPSKA YNGDKRVAIG KSTDVPRDPW VWGSAHPQAQ HTRGSTVAGG FAHLHRGQRL
GGLTEMEHSR QVEQVRHADR LRLHERAVYG LSGVGGPLQP PAVHTDPWSA DSSQSSEGRW
GSHSDSHEED GEVRGYPYGR QSL
