ENAM_PIG
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 25-MAY-2022, entry version 105.
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; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL 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., Tanabe T.,
RA Yamakoshi Y., Murakami C., Dohi N., Shimizu M., 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; 174-276;
RP 515-524; 535-578; 641-646; 663-665; 670-686; 740-750; 765-773 AND 833-848,
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-191 AND SER-216,
RP HYDROXYLATION AT PRO-547, AND GLYCOSYLATION AT ASN-245; ASN-252 AND
RP 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 organization of
CC enamel. Involved in the extension of enamel during the secretory stage
CC of dental enamel formation. {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. Intact
CC enamelin and large-molecular-weight enamelins are limited to the most
CC superficial layer of the developing enamel matrix, while low-molecular-
CC weight enamelins are observed in deeper enamelin. Preferential
CC localization among the crystallites in rod and interrod enamel.
CC {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 secretion.
CC {ECO:0000269|PubMed:9206327}.
CC -!- PTM: Phosphorylated by FAM20C in vitro. {ECO:0000250|UniProtKB:Q9NRM1}.
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DR EMBL; U52196; AAD10837.1; -; mRNA.
DR PIR; T37455; T37455.
DR RefSeq; NP_999406.1; NM_214241.1.
DR AlphaFoldDB; O97939; -.
DR STRING; 9823.ENSSSCP00000009538; -.
DR GlyConnect; 1; 8 N-Linked glycans.
DR iPTMnet; O97939; -.
DR PaxDb; O97939; -.
DR GeneID; 397473; -.
DR KEGG; ssc:397473; -.
DR CTD; 10117; -.
DR eggNOG; ENOG502R69E; Eukaryota.
DR InParanoid; O97939; -.
DR OrthoDB; 201332at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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; Direct protein sequencing; Extracellular matrix;
KW Glycoprotein; Hydroxylation; Phosphoprotein; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..38
FT /evidence="ECO:0000269|PubMed:9206327"
FT CHAIN 39..1142
FT /note="Enamelin"
FT /id="PRO_0000021176"
FT CHAIN 39..665
FT /note="89 kDa enamelin"
FT /id="PRO_0000021177"
FT CHAIN 39..?
FT /note="142 kDa enamelin"
FT /id="PRO_0000021178"
FT CHAIN 39..?
FT /note="155 kDa enamelin"
FT /id="PRO_0000021179"
FT CHAIN 39..?
FT /note="56 kDa enamelin"
FT /id="PRO_0000021180"
FT CHAIN 174..276
FT /note="32 kDa enamelin"
FT /id="PRO_0000021181"
FT PROPEP 277..514
FT /evidence="ECO:0000269|PubMed:9206327"
FT /id="PRO_0000021182"
FT CHAIN 515..665
FT /note="25 kDa enamelin"
FT /id="PRO_0000021183"
FT PROPEP 666..669
FT /evidence="ECO:0000269|PubMed:9206327"
FT /id="PRO_0000021184"
FT CHAIN 670..?
FT /note="34 kDa enamelin"
FT /id="PRO_0000021185"
FT REGION 90..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 374..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 543..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 603..662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 787..820
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 921..965
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1020..1049
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..105
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..146
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..236
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..315
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..392
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..489
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 571..586
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..630
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..662
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0000305"
FT MOD_RES 191
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:9206327"
FT MOD_RES 216
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:9206327"
FT MOD_RES 547
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:9206327"
FT CARBOHYD 245
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:9206327"
FT CARBOHYD 252
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:9206327"
FT CARBOHYD 264
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:9206327"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 462
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 929
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1040
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 680
FT /note="H -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 838..840
FT /note="RDH -> TTI (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
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
