Legends: 1, Phosphoserine. {ECO:0000305}; 2, Phosphoserine. {ECO:0000269|PubMed:9206327}; 3, Hydroxyproline. {ECO:0000269|PubMed:9206327}; 4, N-linked (GlcNAc...). {ECO:0000269|PubMed:9206327}; 5, N-linked (GlcNAc...). {ECO:0000255}; 6, CONFLICT H -> D (in Ref. 2; AA sequence). {ECO:0000305}; 7, SIGNAL {ECO:0000269|PubMed:9206327}; 8, CHAIN 32 kDa enamelin; 9, PROPEP {ECO:0000269|PubMed:9206327}; 10, CHAIN 25 kDa enamelin; 11, CONFLICT RDH -> TTI (in Ref. 2; AA sequence). {ECO:0000305}.
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ID ENAM_PIG Reviewed; 1142 AA.
AC O97939;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 05-OCT-2016, entry version 88.
DE RecName: Full=Enamelin;
DE Contains:
DE RecName: Full=89 kDa enamelin {ECO:0000303|PubMed:9206327};
DE Contains:
DE RecName: Full=142 kDa enamelin {ECO:0000303|PubMed:9206327};
DE Contains:
DE RecName: Full=155 kDa enamelin {ECO:0000303|PubMed:9206327};
DE Contains:
DE RecName: Full=56 kDa enamelin {ECO:0000303|PubMed:9206327};
DE Contains:
DE RecName: Full=32 kDa enamelin {ECO:0000303|PubMed:9206327};
DE Contains:
DE RecName: Full=25 kDa enamelin {ECO:0000303|PubMed:9206327};
DE Contains:
DE RecName: Full=34 kDa enamelin {ECO:0000303|PubMed:9206327};
DE Flags: Precursor;
GN Name=ENAM;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
OC Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RC TISSUE=Enamel epithelium;
RX PubMed=9372788; DOI=10.1177/00220345970760110201;
RA Hu C.-C., Fukae M., Uchida T., Qian Q., Zhang C.H., Ryu O.H.,
RA Tanabe T., Yamakoshi Y., Murakami C., Dohi N., Shimizu M.,
RA Simmer J.P.;
RT "Cloning and characterization of porcine enamelin mRNAs.";
RL J. Dent. Res. 76:1720-1729(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 39-773, PROTEIN SEQUENCE OF 39-49;
RP 174-276; 515-524; 535-578; 641-646; 663-665; 670-686; 740-750; 765-773
RP AND 833-848, FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT
RP SER-191 AND SER-216, HYDROXYLATION AT PRO-547, AND GLYCOSYLATION AT
RP ASN-245; ASN-252 AND ASN-264.
RX PubMed=9206327; DOI=10.1177/08959374960100020201;
RA Fukae M., Tanabe T., Murakami D., Dohi N., Uchida T., Shimizu M.;
RT "Primary structure of the porcine 89 kda enamelin.";
RL Adv. Dent. Res. 10:111-118(1996).
CC -!- FUNCTION: Involved in the mineralization and structural
CC organization of enamel. Involved in the extension of enamel during
CC the secretory stage of dental enamel formation.
CC {ECO:0000269|PubMed:9206327}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000269|PubMed:9206327}.
CC -!- TISSUE SPECIFICITY: Expressed by secretory-phase ameloblasts.
CC Intact enamelin and large-molecular-weight enamelins are limited
CC to the most superficial layer of the developing enamel matrix,
CC while low-molecular-weight enamelins are observed in deeper
CC enamelin. Preferential localization among the crystallites in rod
CC and interrod enamel. {ECO:0000269|PubMed:9372788}.
CC -!- DEVELOPMENTAL STAGE: Expressed from late differentiation to the
CC transition stage. {ECO:0000269|PubMed:9372788}.
CC -!- PTM: Proteolytically cleaved into several smaller polypeptides.
CC Cleavage of N-terminal region of enamelin occurs soon after
CC secretion. {ECO:0000269|PubMed:9206327}.
CC -!- PTM: Phosphorylated by FAM20C in vitro.
CC {ECO:0000250|UniProtKB:Q9NRM1}.
DR EMBL; U52196; AAD10837.1; -; mRNA.
DR PIR; T37455; T37455.
DR RefSeq; NP_999406.1; NM_214241.1.
DR UniGene; Ssc.748; -.
DR STRING; 9823.ENSSSCP00000009538; -.
DR iPTMnet; O97939; -.
DR UniCarbKB; O97939; -.
DR PaxDb; O97939; -.
DR PRIDE; O97939; -.
DR GeneID; 397473; -.
DR KEGG; ssc:397473; -.
DR CTD; 10117; -.
DR eggNOG; ENOG410IEBP; Eukaryota.
DR eggNOG; ENOG410YWPJ; LUCA.
DR HOGENOM; HOG000112367; -.
DR HOVERGEN; HBG005585; -.
DR InParanoid; O97939; -.
DR PMAP-CutDB; O97939; -.
DR Proteomes; UP000008227; Unplaced.
DR GO; GO:0005578; C:proteinaceous extracellular matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0031214; P:biomineral tissue development; IEA:UniProtKB-KW.
DR InterPro; IPR015673; Enamelin.
DR PANTHER; PTHR16784; PTHR16784; 1.
DR Pfam; PF15362; Enamelin; 1.
PE 1: Evidence at protein level;
KW Biomineralization; Complete proteome; Direct protein sequencing;
KW Extracellular matrix; Glycoprotein; Hydroxylation; Phosphoprotein;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1 38 {ECO:0000269|PubMed:9206327}.
FT CHAIN 39 1142 Enamelin.
FT /FTId=PRO_0000021176.
FT CHAIN 39 665 89 kDa enamelin.
FT /FTId=PRO_0000021177.
FT CHAIN 39 ? 142 kDa enamelin.
FT /FTId=PRO_0000021178.
FT CHAIN 39 ? 155 kDa enamelin.
FT /FTId=PRO_0000021179.
FT CHAIN 39 ? 56 kDa enamelin.
FT /FTId=PRO_0000021180.
FT CHAIN 174 276 32 kDa enamelin.
FT /FTId=PRO_0000021181.
FT PROPEP 277 514 {ECO:0000269|PubMed:9206327}.
FT /FTId=PRO_0000021182.
FT CHAIN 515 665 25 kDa enamelin.
FT /FTId=PRO_0000021183.
FT PROPEP 666 669 {ECO:0000269|PubMed:9206327}.
FT /FTId=PRO_0000021184.
FT CHAIN 670 ? 34 kDa enamelin.
FT /FTId=PRO_0000021185.
FT MOD_RES 53 53 Phosphoserine. {ECO:0000305}.
FT MOD_RES 191 191 Phosphoserine.
FT {ECO:0000269|PubMed:9206327}.
FT MOD_RES 216 216 Phosphoserine.
FT {ECO:0000269|PubMed:9206327}.
FT MOD_RES 547 547 Hydroxyproline.
FT {ECO:0000269|PubMed:9206327}.
FT CARBOHYD 245 245 N-linked (GlcNAc...).
FT {ECO:0000269|PubMed:9206327}.
FT CARBOHYD 252 252 N-linked (GlcNAc...).
FT {ECO:0000269|PubMed:9206327}.
FT CARBOHYD 264 264 N-linked (GlcNAc...).
FT {ECO:0000269|PubMed:9206327}.
FT CARBOHYD 291 291 N-linked (GlcNAc...). {ECO:0000255}.
FT CARBOHYD 462 462 N-linked (GlcNAc...). {ECO:0000255}.
FT CARBOHYD 929 929 N-linked (GlcNAc...). {ECO:0000255}.
FT CARBOHYD 1040 1040 N-linked (GlcNAc...). {ECO:0000255}.
FT CONFLICT 680 680 H -> D (in Ref. 2; AA sequence).
FT {ECO:0000305}.
FT CONFLICT 838 840 RDH -> TTI (in Ref. 2; AA sequence).
FT {ECO:0000305}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 213 1114 ipfam:Enamelin [T]
SQ SEQUENCE 1142 AA; 128352 MW; 938306BC87CC5FC6 CRC64;
MLLSCRHGAS SPKLDNLVPS GKMKILLVFL GLLCYSAAMP MQMPRMPGFS SKSEEMMRYG
HFNFMNAPHM AHLGTLYGNG MQLPQFFPQY QMPMWPQPPP NKKHPQKPSA SKQQSKTDPA
PESQKPNQPQ PKTPTPKQPL NEPSPTPTQP EEETQTPQAF PPFGNGLFPY QQPLWHVPHR
IPPGYGRPPT SNEEGGNPYF GFFGYHGFGG RPPYYSEEMF EQDFEKPKEK DPPKTETPAT
EPSVNTTVPE TNSTQPNAPN PRGNDTSPTG TSGQGPNPRS NPTGQNGPAV NVSGQGVPRS
QSPWGPRQTI IHENYPNPNI RGFPARRQWR PPGPAMGHRR NGPFYRNQQI QRGPRWNSFT
LEGKQAVRPG YPTYRRVYGS TARSNPPNYA GNSANLRRKP EGPNKNPMVT NVAPPGPKHG
TVDQNENIQN PREKQVSQKE RTVVPTRDPS GPWRNSQDYG INKSNYKLPQ PEDNMLVPNF
NSIDQRENSY YPRGESKRAP NSDGQTQTQI IPKGIVLEPR RIPYESETNQ PELKHSAYQP
VYTEGIPSPA KEHFPAGRNT WNQQEISPPF KEDPGRQEEH LPHLSHGSRV HVYYPDYNPY
DPRENSPYLR SNTWYERDDS PNTMGQPENP HYPMNTPDPK ETIPYNEEDP IDPTGDEHFP
GQSRWDMEEL SFKEDPTVRH YEGEQYTSNQ PKEYLPYSLD NPSKPREDFL YGEFYPWNPE
ENFPSYNTAP TVSSPVESRG YYANNAVGQE ESTMFPSWSS WDPRIQAQGQ KEGRPYLNRN
FWDQSTNLYK TPTSSPHQKE NQPYSNNSPA GLQKNPTWHE GENLNYGMQI TRLNSPERDH
LAFPDLIPPD YPGGQKESHV FHLSQRGPCC AGGSMWPKNN PLALQDYTQS FGLAPGENPD
TSIGYAEDSH IKYARQTVSP TSIVPGQRNS SEKILPGESQ NPSPFKDDVS TLRRSTPCSV
KSQLSQRGIM PLPEANSLQS KNTPCLTSDL GGDGNNVLEQ IFEGNQLNER TVDLTPEQLV
FGTPDKEPRP EGIPNEMQGN ESERQQQRQS SILQLPCFGS KLANYHTSSI GTPSSLGRQD
SFDGDPIMPT ETPNSLAGLA TGAQFQNINV DPLNEDEHTP FDSLQIGTNP QDQVQDCLLL
QA
//
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