ELN_BOVIN
ID ELN_BOVIN Reviewed; 747 AA.
AC P04985; P04986; P04987; Q28096; Q28097; Q28098; Q28099; Q28101; Q29421;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=Elastin;
DE AltName: Full=Tropoelastin;
DE Flags: Precursor;
GN Name=ELN;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND ALLYSINE AT LYS-105; LYS-109; LYS-252;
RP LYS-271; LYS-275; LYS-324; LYS-327; LYS-400; LYS-404; LYS-407; LYS-445;
RP LYS-448; LYS-489; LYS-493; LYS-544; LYS-548; LYS-552; LYS-606; LYS-609;
RP LYS-645; LYS-649; LYS-685 AND LYS-688.
RX PubMed=3032943; DOI=10.1016/s0021-9258(18)45639-6;
RA Raju K., Anwar R.A.;
RT "Primary structures of bovine elastin a, b, and c deduced from the
RT sequences of cDNA clones.";
RL J. Biol. Chem. 262:5755-5762(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-27.
RC TISSUE=Nuchal ligament;
RX PubMed=2543440; DOI=10.1021/bi00432a003;
RA Yeh H., Anderson N., Ornstein-Goldstein N., Bashir M.M., Rosenbloom J.C.,
RA Abrams W.R., Indik Z., Yoon K., Parks W., Mecham R., Rosenbloom J.;
RT "Structure of the bovine elastin gene and S1 nuclease analysis of
RT alternative splicing of elastin mRNA in the bovine nuchal ligament.";
RL Biochemistry 28:2365-2370(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-27.
RX PubMed=2031719; DOI=10.1139/o91-027;
RA Manohar A., Shi W., Anwar R.A.;
RT "Partial characterization of bovine elastin gene; comparison with the gene
RT for human elastin.";
RL Biochem. Cell Biol. 69:185-192(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 54-747 (ISOFORMS 4; 5; 6 AND 7).
RX PubMed=2992576; DOI=10.1021/bi00334a001;
RA Cicila G., May M., Ornstein-Goldstein N., Indik Z., Morrow S., Yeh H.S.,
RA Rosenbloom J., Boyd C., Rosenbloom J., Yoon K.;
RT "Structure of the 3' portion of the bovine elastin gene.";
RL Biochemistry 24:3075-3080(1985).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 54-747 (ISOFORMS 4; 5; 6 AND 7).
RX PubMed=3665402; DOI=10.1016/s0174-173x(87)80030-4;
RA Yeh H., Ornstein-Goldstein N., Indik Z., Sheppard P., Anderson N.,
RA Rosenbloom J.C., Cicila G., Yoon K., Rosenbloom J.;
RT "Sequence variation of bovine elastin mRNA due to alternative splicing.";
RL Coll. Relat. Res. 7:235-247(1987).
RN [6]
RP NUCLEOTIDE SEQUENCE OF 678-747.
RX PubMed=6150137;
RA Rosenbloom J.;
RT "Elastin: relation of protein and gene structure to disease.";
RL Lab. Invest. 51:605-623(1984).
RN [7]
RP DISULFIDE BOND.
RX PubMed=1632791; DOI=10.1016/s0006-291x(05)80843-5;
RA Brown P.L., Mecham L., Tisdale C., Mecham R.P.;
RT "The cysteine residues in the carboxy terminal domain of tropoelastin form
RT an intrachain disulfide bond that stabilizes a loop structure and
RT positively charged pocket.";
RL Biochem. Biophys. Res. Commun. 186:549-555(1992).
RN [8]
RP INTERACTION WITH BGN AND MFAP2.
RX PubMed=11723132; DOI=10.1074/jbc.m109540200;
RA Reinboth B., Hanssen E., Cleary E.G., Gibson M.A.;
RT "Molecular interactions of biglycan and decorin with elastic fiber
RT components: biglycan forms a ternary complex with tropoelastin and
RT microfibril-associated glycoprotein 1.";
RL J. Biol. Chem. 277:3950-3957(2002).
RN [9]
RP INTERACTION WITH EFEMP2.
RX PubMed=16478991; DOI=10.1128/mcb.26.5.1700-1709.2006;
RA McLaughlin P.J., Chen Q., Horiguchi M., Starcher B.C., Stanton J.B.,
RA Broekelmann T.J., Marmorstein A.D., McKay B., Mecham R., Nakamura T.,
RA Marmorstein L.Y.;
RT "Targeted disruption of fibulin-4 abolishes elastogenesis and causes
RT perinatal lethality in mice.";
RL Mol. Cell. Biol. 26:1700-1709(2006).
RN [10]
RP INTERACTION WITH MFAP4.
RX PubMed=26601954; DOI=10.1074/jbc.m115.681775;
RA Pilecki B., Holm A.T., Schlosser A., Moeller J.B., Wohl A.P., Zuk A.V.,
RA Heumueller S.E., Wallis R., Moestrup S.K., Sengle G., Holmskov U.,
RA Sorensen G.L.;
RT "Characterization of microfibrillar-associated protein 4 (MFAP4) as a
RT tropoelastin- and fibrillin-binding protein involved in elastic fiber
RT formation.";
RL J. Biol. Chem. 291:1103-1114(2016).
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:P54320}.
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 (PubMed:11723132).
CC Interacts with FBLN5 and FBN1. Forms a ternary complex with FBN1 and
CC FBLN2 or FBLN5 (By similarity). Interacts with MFAP4 in a Ca (2+)-
CC dependent manner; this interaction promotes ELN self-assembly
CC (PubMed:26601954, PubMed:11723132) (By similarity). Interacts with
CC EFEMP2 with moderate affinity (PubMed:16478991).
CC {ECO:0000250|UniProtKB:P15502, ECO:0000269|PubMed:11723132,
CC ECO:0000269|PubMed:16478991, ECO:0000269|PubMed:26601954}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1; Synonyms=A;
CC IsoId=P04985-1; Sequence=Displayed;
CC Name=2; Synonyms=B;
CC IsoId=P04985-2; Sequence=VSP_004239;
CC Name=3; Synonyms=C;
CC IsoId=P04985-3; Sequence=VSP_004240;
CC Name=4;
CC IsoId=P04985-4; Sequence=VSP_011943;
CC Name=5; Synonyms=Elastin-cBEL2;
CC IsoId=P04985-5; Sequence=VSP_011941;
CC Name=6; Synonyms=Elastin-cBEL3;
CC IsoId=P04985-6; Sequence=VSP_004240, VSP_011940;
CC Name=7; Synonyms=Elastin-cBEL1;
CC IsoId=P04985-7; Sequence=VSP_004240, VSP_011942, VSP_011943;
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; J02717; AAA30503.1; -; mRNA.
DR EMBL; K03505; AAA30505.1; -; mRNA.
DR EMBL; K03506; AAA30506.1; -; mRNA.
DR EMBL; J02855; AAA30776.1; -; Genomic_DNA.
DR EMBL; M58652; AAA03519.2; -; Genomic_DNA.
DR EMBL; M19372; AAA30498.1; -; Genomic_DNA.
DR EMBL; M11422; AAA30498.1; JOINED; Genomic_DNA.
DR EMBL; M19366; AAA30498.1; JOINED; Genomic_DNA.
DR EMBL; M19367; AAA30498.1; JOINED; Genomic_DNA.
DR EMBL; M19368; AAA30498.1; JOINED; Genomic_DNA.
DR EMBL; M19369; AAA30498.1; JOINED; Genomic_DNA.
DR EMBL; M19370; AAA30498.1; JOINED; Genomic_DNA.
DR EMBL; M19371; AAA30498.1; JOINED; Genomic_DNA.
DR EMBL; M22771; AAA30498.1; JOINED; Genomic_DNA.
DR EMBL; M22772; AAA30498.1; JOINED; Genomic_DNA.
DR EMBL; M22773; AAA30498.1; JOINED; Genomic_DNA.
DR EMBL; M22774; AAA30498.1; JOINED; Genomic_DNA.
DR EMBL; M22775; AAA30498.1; JOINED; Genomic_DNA.
DR EMBL; M22988; AAA30498.1; JOINED; Genomic_DNA.
DR EMBL; M23010; AAA30498.1; JOINED; Genomic_DNA.
DR EMBL; M19372; AAA30499.1; -; Genomic_DNA.
DR EMBL; M11422; AAA30499.1; JOINED; Genomic_DNA.
DR EMBL; M19366; AAA30499.1; JOINED; Genomic_DNA.
DR EMBL; M19368; AAA30499.1; JOINED; Genomic_DNA.
DR EMBL; M19369; AAA30499.1; JOINED; Genomic_DNA.
DR EMBL; M19370; AAA30499.1; JOINED; Genomic_DNA.
DR EMBL; M19371; AAA30499.1; JOINED; Genomic_DNA.
DR EMBL; M22771; AAA30499.1; JOINED; Genomic_DNA.
DR EMBL; M22772; AAA30499.1; JOINED; Genomic_DNA.
DR EMBL; M22773; AAA30499.1; JOINED; Genomic_DNA.
DR EMBL; M22774; AAA30499.1; JOINED; Genomic_DNA.
DR EMBL; M22775; AAA30499.1; JOINED; Genomic_DNA.
DR EMBL; M22988; AAA30499.1; JOINED; Genomic_DNA.
DR EMBL; M23010; AAA30499.1; JOINED; Genomic_DNA.
DR EMBL; M19372; AAA30500.1; -; Genomic_DNA.
DR EMBL; M11422; AAA30500.1; JOINED; Genomic_DNA.
DR EMBL; M19366; AAA30500.1; JOINED; Genomic_DNA.
DR EMBL; M19367; AAA30500.1; JOINED; Genomic_DNA.
DR EMBL; M19368; AAA30500.1; JOINED; Genomic_DNA.
DR EMBL; M19369; AAA30500.1; JOINED; Genomic_DNA.
DR EMBL; M19370; AAA30500.1; JOINED; Genomic_DNA.
DR EMBL; M19371; AAA30500.1; JOINED; Genomic_DNA.
DR EMBL; M22771; AAA30500.1; JOINED; Genomic_DNA.
DR EMBL; M22772; AAA30500.1; JOINED; Genomic_DNA.
DR EMBL; M22773; AAA30500.1; JOINED; Genomic_DNA.
DR EMBL; M22774; AAA30500.1; JOINED; Genomic_DNA.
DR EMBL; M22988; AAA30500.1; JOINED; Genomic_DNA.
DR EMBL; M19372; AAA30501.1; -; Genomic_DNA.
DR EMBL; M11422; AAA30501.1; JOINED; Genomic_DNA.
DR EMBL; M19366; AAA30501.1; JOINED; Genomic_DNA.
DR EMBL; M19367; AAA30501.1; JOINED; Genomic_DNA.
DR EMBL; M19368; AAA30501.1; JOINED; Genomic_DNA.
DR EMBL; M19369; AAA30501.1; JOINED; Genomic_DNA.
DR EMBL; M19370; AAA30501.1; JOINED; Genomic_DNA.
DR EMBL; M19371; AAA30501.1; JOINED; Genomic_DNA.
DR EMBL; M22771; AAA30501.1; JOINED; Genomic_DNA.
DR EMBL; M22772; AAA30501.1; JOINED; Genomic_DNA.
DR EMBL; M22773; AAA30501.1; JOINED; Genomic_DNA.
DR EMBL; M22774; AAA30501.1; JOINED; Genomic_DNA.
DR EMBL; M22775; AAA30501.1; JOINED; Genomic_DNA.
DR EMBL; M22988; AAA30501.1; JOINED; Genomic_DNA.
DR EMBL; M31898; AAA96417.1; -; Genomic_DNA.
DR EMBL; M31894; AAA96417.1; JOINED; Genomic_DNA.
DR EMBL; M31895; AAA96417.1; JOINED; Genomic_DNA.
DR EMBL; M31896; AAA96417.1; JOINED; Genomic_DNA.
DR EMBL; M31897; AAA96417.1; JOINED; Genomic_DNA.
DR PIR; A31865; EABO.
DR AlphaFoldDB; P04985; -.
DR CORUM; P04985; -.
DR DIP; DIP-35453N; -.
DR IntAct; P04985; 4.
DR PRIDE; P04985; -.
DR eggNOG; ENOG502RYNR; Eukaryota.
DR InParanoid; P04985; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IEA:InterPro.
DR GO; GO:0071953; C:elastic fiber; IDA:AgBase.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IEA:InterPro.
DR DisProt; DP01801; -.
DR InterPro; IPR003979; Tropoelastin.
DR PANTHER; PTHR24018; PTHR24018; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Disulfide bond; Extracellular matrix; Hydroxylation;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000250|UniProtKB:Q99372"
FT CHAIN 27..747
FT /note="Elastin"
FT /id="PRO_0000021161"
FT MOD_RES 34
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 65
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 87
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 105
FT /note="Allysine"
FT /evidence="ECO:0000269|PubMed:3032943"
FT MOD_RES 109
FT /note="Allysine"
FT /evidence="ECO:0000269|PubMed:3032943"
FT MOD_RES 165
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 178
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 181
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 188
FT /note="Hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 201
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 252
FT /note="Allysine"
FT /evidence="ECO:0000269|PubMed:3032943"
FT MOD_RES 271
FT /note="Allysine"
FT /evidence="ECO:0000269|PubMed:3032943"
FT MOD_RES 275
FT /note="Allysine"
FT /evidence="ECO:0000269|PubMed:3032943"
FT MOD_RES 298
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 302
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 324
FT /note="Allysine"
FT /evidence="ECO:0000269|PubMed:3032943"
FT MOD_RES 327
FT /note="Allysine"
FT /evidence="ECO:0000269|PubMed:3032943"
FT MOD_RES 335
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 365
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 370
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 375
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 380
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 385
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 400
FT /note="Allysine"
FT /evidence="ECO:0000269|PubMed:3032943"
FT MOD_RES 404
FT /note="Allysine"
FT /evidence="ECO:0000269|PubMed:3032943"
FT MOD_RES 407
FT /note="Allysine"
FT /evidence="ECO:0000269|PubMed:3032943"
FT MOD_RES 445
FT /note="Allysine"
FT /evidence="ECO:0000269|PubMed:3032943"
FT MOD_RES 448
FT /note="Allysine"
FT /evidence="ECO:0000269|PubMed:3032943"
FT MOD_RES 462
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 478
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 489
FT /note="Allysine"
FT /evidence="ECO:0000269|PubMed:3032943"
FT MOD_RES 493
FT /note="Allysine"
FT /evidence="ECO:0000269|PubMed:3032943"
FT MOD_RES 513
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 544
FT /note="Allysine"
FT /evidence="ECO:0000269|PubMed:3032943"
FT MOD_RES 548
FT /note="Allysine"
FT /evidence="ECO:0000269|PubMed:3032943"
FT MOD_RES 552
FT /note="Allysine"
FT /evidence="ECO:0000269|PubMed:3032943"
FT MOD_RES 566
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 575
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 584
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 593
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 599
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 606
FT /note="Allysine"
FT /evidence="ECO:0000269|PubMed:3032943"
FT MOD_RES 609
FT /note="Allysine"
FT /evidence="ECO:0000269|PubMed:3032943"
FT MOD_RES 630
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 645
FT /note="Allysine"
FT /evidence="ECO:0000269|PubMed:3032943"
FT MOD_RES 649
FT /note="Allysine"
FT /evidence="ECO:0000269|PubMed:3032943"
FT MOD_RES 685
FT /note="Allysine"
FT /evidence="ECO:0000269|PubMed:3032943"
FT MOD_RES 688
FT /note="Allysine"
FT /evidence="ECO:0000269|PubMed:3032943"
FT MOD_RES 719
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 733
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT DISULFID 737..742
FT /evidence="ECO:0000269|PubMed:1632791"
FT VAR_SEQ 226..259
FT /note="Missing (in isoform 3, isoform 6 and isoform 7)"
FT /evidence="ECO:0000305"
FT /id="VSP_004240"
FT VAR_SEQ 226..239
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_004239"
FT VAR_SEQ 499
FT /note="L -> LALLAFAGL (in isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_011940"
FT VAR_SEQ 598..610
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_011941"
FT VAR_SEQ 654..676
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000305"
FT /id="VSP_011942"
FT VAR_SEQ 708
FT /note="G -> GVAARPGFGLSPIFPG (in isoform 4 and isoform 7)"
FT /evidence="ECO:0000305"
FT /id="VSP_011943"
FT CONFLICT 1..3
FT /note="MRS -> MAG (in Ref. 2 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 12
FT /note="E -> G (in Ref. 2 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 78..80
FT /note="EGS -> GLG (in Ref. 4 and 5)"
FT /evidence="ECO:0000305"
FT CONFLICT 89..97
FT /note="GFFGAGGGA -> ALVPGGP (in Ref. 4 and 5)"
FT /evidence="ECO:0000305"
FT CONFLICT 191..194
FT /note="QVGA -> PGGG (in Ref. 4 and 5)"
FT /evidence="ECO:0000305"
FT CONFLICT 213
FT /note="L -> V (in Ref. 4 and 5)"
FT /evidence="ECO:0000305"
FT CONFLICT 292
FT /note="P -> A (in Ref. 4 and 5)"
FT /evidence="ECO:0000305"
FT CONFLICT 334
FT /note="L -> F (in Ref. 4 and 5)"
FT /evidence="ECO:0000305"
FT CONFLICT 393
FT /note="L -> V (in Ref. 4 and 5)"
FT /evidence="ECO:0000305"
FT CONFLICT 398
FT /note="T -> A (in Ref. 4 and 5)"
FT /evidence="ECO:0000305"
FT CONFLICT 413
FT /note="A -> G (in Ref. 4 and 5)"
FT /evidence="ECO:0000305"
FT CONFLICT 424
FT /note="L -> V (in Ref. 4 and 5)"
FT /evidence="ECO:0000305"
FT CONFLICT 439
FT /note="P -> Q (in Ref. 4 and 5)"
FT /evidence="ECO:0000305"
FT CONFLICT 460
FT /note="V -> L (in Ref. 4 and 5)"
FT /evidence="ECO:0000305"
FT CONFLICT 471
FT /note="L -> V (in Ref. 4 and 5)"
FT /evidence="ECO:0000305"
FT CONFLICT 572
FT /note="A -> V (in Ref. 4 and 5)"
FT /evidence="ECO:0000305"
FT CONFLICT 581
FT /note="A -> V (in Ref. 4 and 5)"
FT /evidence="ECO:0000305"
FT CONFLICT 595
FT /note="P -> F (in Ref. 4 and 5)"
FT /evidence="ECO:0000305"
FT CONFLICT 637
FT /note="V -> G (in Ref. 4 and 5)"
FT /evidence="ECO:0000305"
FT CONFLICT 681
FT /note="Missing (in Ref. 6)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 747 AA; 64229 MW; 633C03E411643D83 CRC64;
MRSLTAAARR PEVLLLLLCI LQPSQPGGVP GAVPGGVPGG VFFPGAGLGG LGVGGLGPGV
KPAKPGVGGL VGPGLGAEGS ALPGAFPGGF FGAGGGAAGA AAAYKAAAKA GAAGLGVGGI
GGVGGLGVST GAVVPQLGAG VGAGVKPGKV PGVGLPGVYP GGVLPGAGAR FPGIGVLPGV
PTGAGVKPKA QVGAGAFAGI PGVGPFGGQQ PGLPLGYPIK APKLPAGYGL PYKTGKLPYG
FGPGGVAGSA GKAGYPTGTG VGPQAAAAAA KAAAKLGAGG AGVLPGVGVG GPGIPGAPGA
IPGIGGIAGV GAPDAAAAAA AAAKAAKFGA AGGLPGVGVP GVGVPGVGVP GVGVPGVGVP
GVGVPGVGVP GVGVPGVGVP GVGVPGVGVP GALSPAATAK AAAKAAKFGA RGAVGIGGIP
TFGLGPGGFP GIGDAAAAPA AAAAKAAKIG AGGVGALGGV VPGAPGAIPG LPGVGGVPGV
GIPAAAAAKA AAKAAQFGLG PGVGVAPGVG VVPGVGVVPG VGVAPGIGLG PGGVIGAGVP
AAAKSAAKAA AKAQFRAAAG LPAGVPGLGV GAGVPGLGVG AGVPGLGVGA GVPGPGAVPG
TLAAAKAAKF GPGGVGALGG VGDLGGAGIP GGVAGVVPAA AAAAKAAAKA AQFGLGGVGG
LGVGGLGAVP GAVGLGGVSP AAAAKAAKFG AAGLGGVLGA GQPFPIGGGA GGLGVGGKPP
KPFGGALGAL GFPGGACLGK SCGRKRK
