ID   ELN_SHEEP               Reviewed;         100 AA.
AC   P11547;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   25-MAY-2022, entry version 67.
DE   RecName: Full=Elastin;
DE   AltName: Full=Tropoelastin;
DE   Flags: Fragment;
GN   Name=ELN;
OS   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Ovis.
OX   NCBI_TaxID=9940;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX   PubMed=3839997; DOI=10.1016/0003-9861(85)90595-8;
RA   Yoon K., Davidson J.M., Boyd C., May M., LuValle P., Ornstein-Goldstein N.,
RA   Smith J., Indik Z., Ross A., Golub E., Rosenbloom J.;
RT   "Analysis of the 3' region of the sheep elastin gene.";
RL   Arch. Biochem. Biophys. 241:684-691(1985).
CC   -!- FUNCTION: Major structural protein of tissues such as aorta and nuchal
CC       ligament, which must expand rapidly and recover completely. Molecular
CC       determinant of the late arterial morphogenesis, stabilizing arterial
CC       structure by regulating proliferation and organization of vascular
CC       smooth muscle (By similarity). {ECO:0000250|UniProtKB:Q9WVH9}.
CC   -!- SUBUNIT: The polymeric elastin chains are cross-linked together into an
CC       extensible 3D network. Forms a ternary complex with BGN and MFAP2.
CC       Interacts with MFAP2 via divalent cations (calcium > magnesium >
CC       manganese) in a dose-dependent and saturating manner. Interacts with
CC       FBLN5 and FBN1. Forms a ternary complex with FBN1 and FBLN2 or FBLN5.
CC       Interacts with MFAP4 in a Ca (2+)-dependent manner; this interaction
CC       promotes ELN self-assembly (By similarity). Interacts with EFEMP2 with
CC       moderate affinity (By similarity). {ECO:0000250|UniProtKB:P04985,
CC       ECO:0000250|UniProtKB:P15502}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000250|UniProtKB:P15502}. Note=Extracellular matrix of
CC       elastic fibers. {ECO:0000250|UniProtKB:P15502}.
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: 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; M26188; AAA31515.1; ALT_SEQ; mRNA.
DR   EMBL; M26189; AAA31516.1; -; Genomic_DNA.
DR   PIR; S59623; S59623.
DR   AlphaFoldDB; P11547; -.
DR   Proteomes; UP000002356; 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; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Extracellular matrix; Hydroxylation; Reference proteome;
KW   Repeat; Secreted.
FT   CHAIN           <1..100
FT                   /note="Elastin"
FT                   /id="PRO_0000086957"
FT   MOD_RES         72
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         86
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250"
FT   DISULFID        90..95
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   100 AA;  8662 MW;  5C680C6A5AEE6786 CRC64;
     FGLGGVGGLG VGGLGVGGLG AVPGAVGLGG VSPAAAAKAA KFGAAGLGGV LGAGRPFPIG
     GGAGGLGVGG KPPKPFGGAL GALGFPGGAC LGKSCGRKRK