ELN_CHICK
ID ELN_CHICK Reviewed; 750 AA.
AC P07916;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=Elastin;
DE AltName: Full=Tropoelastin;
DE Flags: Precursor; Fragment;
GN Name=ELN;
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]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3593675; DOI=10.1021/bi00380a001;
RA Bressan G.M., Argos P., Stanley K.K.;
RT "Repeating structure of chick tropoelastin revealed by complementary DNA
RT cloning.";
RL Biochemistry 26:1497-1503(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 85-750 (ISOFORM 2).
RX PubMed=2841924; DOI=10.1016/0006-291x(88)90247-1;
RA Baule V.J., Foster J.A.;
RT "Multiple chick tropoelastin mRNAs.";
RL Biochem. Biophys. Res. Commun. 154:1054-1060(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 457-750.
RC TISSUE=Aorta;
RX PubMed=3502711; DOI=10.1016/0003-9861(87)90602-3;
RA Tokimitsu I., Tajima S., Nishikawa T., Tajima M., Fukasawa T.;
RT "Sequence analysis of elastin cDNA from chick aorta and tissue-specific
RT transcription of the elastin gene in developing chick embryo.";
RL Arch. Biochem. Biophys. 256:455-461(1987).
RN [4]
RP HYDROXYLATION.
RX PubMed=6696746; DOI=10.1042/bj2170581;
RA Rich C.B., Foster J.A.;
RT "Isolation of tropoelastin a from lathyritic chick aortae.";
RL Biochem. J. 217:581-584(1984).
CC -!- FUNCTION: Major structural protein of tissues such as aorta and nuchal
CC ligament, which must expand rapidly and recover completely.
CC -!- SUBUNIT: The polymeric elastin chains are cross-linked together into an
CC extensible 3D network.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix. Note=Extracellular matrix of elastic fibers.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=P07916-1; Sequence=Displayed;
CC Name=2; Synonyms=Embryonic;
CC IsoId=P07916-2; Sequence=VSP_004241, VSP_004242;
CC -!- PTM: Elastin is formed through the cross-linking of its soluble
CC precursor tropoelastin. Cross-linking is initiated through the action
CC of lysyl oxidase on exposed lysines to form allysine. Subsequent
CC spontaneous condensation reactions with other allysine or unmodified
CC lysine residues result in various bi-, tri-, and tetrafunctional cross-
CC links. The most abundant cross-links in mature elastin fibers are
CC lysinonorleucine, allysine aldol, desmosine, and isodesmosine.
CC -!- PTM: Hydroxylated on proline residues. {ECO:0000269|PubMed:6696746}.
CC -!- PTM: Hydroxylation on proline residues within the sequence motif, GXPG,
CC is most likely to be 4-hydroxy as this fits the requirement for 4-
CC hydroxylation in vertebrates. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the elastin family. {ECO:0000305}.
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DR EMBL; M18633; AAA48761.1; -; mRNA.
DR EMBL; M21880; AAA49082.1; -; mRNA.
DR EMBL; M15889; AAA49108.1; -; mRNA.
DR PIR; A26601; A26601.
DR AlphaFoldDB; P07916; -.
DR STRING; 9031.ENSGALP00000001601; -.
DR PaxDb; P07916; -.
DR PRIDE; P07916; -.
DR eggNOG; ENOG502RYNR; Eukaryota.
DR InParanoid; P07916; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IEA:InterPro.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IEA:InterPro.
DR InterPro; IPR003979; Tropoelastin.
DR PANTHER; PTHR24018; PTHR24018; 4.
PE 1: Evidence at protein level;
KW Alternative splicing; Disulfide bond; Extracellular matrix; Hydroxylation;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL <1..24
FT CHAIN 25..750
FT /note="Elastin"
FT /id="PRO_0000021162"
FT REPEAT 83..127
FT /note="1"
FT REPEAT 219..262
FT /note="2"
FT REPEAT 263..318
FT /note="3"
FT REPEAT 319..393
FT /note="4"
FT REPEAT 394..482
FT /note="5"
FT REPEAT 483..554
FT /note="6"
FT REPEAT 555..619
FT /note="7"
FT REPEAT 620..686
FT /note="8"
FT REGION 83..686
FT /note="8 X tandem repeats"
FT MOD_RES 32
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 67
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 102
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 176
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 189
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 192
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 211
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 276
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 345
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 363
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 368
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 441
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 455
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 480
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 576
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 635
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 720
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT DISULFID 739..745
FT /evidence="ECO:0000250"
FT VAR_SEQ 212
FT /note="G -> GLGGFGGQQPGVPLGYPIKAPKLPG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:2841924"
FT /id="VSP_004241"
FT VAR_SEQ 501
FT /note="G -> GVGVPGVGVPG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:2841924"
FT /id="VSP_004242"
FT CONFLICT 536
FT /note="A -> G (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 571
FT /note="G -> A (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 610
FT /note="P -> A (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 654
FT /note="A -> R (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 667
FT /note="P -> R (in Ref. 3)"
FT /evidence="ECO:0000305"
FT NON_TER 1
SQ SEQUENCE 750 AA; 63696 MW; E57ECD60C6EE556F CRC64;
ARQAAAPLLP GVLLLFSILP ASQQGGVPGA IPGGGVPGGG FFPGAGVGGL GAGLGAGLGA
GGKPLKPGVS GLGGLGPLGL QPGAGVGGLG AGLGAFPGAA FPGAASAAAL KAAAKAGAGL
GGVGGIGGLG GVGGVGVPGG LGVPGVVQPG VGAAGKPPKV PGAGIPGAFP GGGVLPGAGI
RFPGVGVLPG VPTGTGIKAK GPGAGAFAGI PGGYRLPFVN GLGPGGIGAG VLAGKAGYPT
GTGVGAQAAA AKAAAKYGAG VLPGAGGIPG VGGVVPGVGV VPGAGVGGPA AAAAAAKAAA
KAGAYGAGVL PGAGGVPGVV PGVGVVPGLV PGVGGIPGVA GVGTPAGAAA AAAKAAKYGA
GVPGVGVPGV GIGGVPGVPG VPGVPGVPGV PGVPGVPGVP GVPGVPGVPG VVPGVGVGGP
AAAAAAKAAA KAAAFGAGRV PGVGVPGAVP GVGVPGVGVP GVGVPGVGVP GVGVPGVGVP
GVGVPGVGVP GVGVPGVGVP GLVPGAGPAA AAKAAAKAAK YGAGGLAPGV GGLAPAVGGL
APGVGGLVPG VGGLVPGVGG LAPGVGGLAP GVGAVPGVGG PAAAAKAAAK AAKYGAGVGG
VPGAVPGAVP GVPGVPGVTP GVGGVPSLVP GVGVPGVGVL PGAGIPQVGV QPGAKPPKFG
VPGAGVPGVG GIPGGLGVGG LGVGGLGAGG LGAGVGVPGF GVSPIFPGGV GGQLGFGGKP
PKTYGGALGA LGFRGGVGCA QGKYCGRKRK
