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Database: UniProt
Entry: A0A7J7ZU59_MYOMY
LinkDB: A0A7J7ZU59_MYOMY
Original site: A0A7J7ZU59_MYOMY 
ID   A0A7J7ZU59_MYOMY        Unreviewed;       573 AA.
AC   A0A7J7ZU59;
DT   07-APR-2021, integrated into UniProtKB/TrEMBL.
DT   07-APR-2021, sequence version 1.
DT   08-OCT-2025, entry version 14.
DE   SubName: Full=Collagen type XVIII alpha 1 chain {ECO:0000313|EMBL:KAF6377619.1};
GN   ORFNames=mMyoMyo1_003131 {ECO:0000313|EMBL:KAF6377619.1};
OS   Myotis myotis (Greater mouse-eared bat) (Vespertilio myotis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Yangochiroptera; Vespertilionidae;
OC   Myotis.
OX   NCBI_TaxID=51298 {ECO:0000313|EMBL:KAF6377619.1, ECO:0000313|Proteomes:UP000527355};
RN   [1] {ECO:0000313|EMBL:KAF6377619.1, ECO:0000313|Proteomes:UP000527355}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MMyoMyo1 {ECO:0000313|EMBL:KAF6377619.1};
RC   TISSUE=Flight muscle {ECO:0000313|EMBL:KAF6377619.1};
RX   PubMed=32699395;
RA   Jebb D., Huang Z., Pippel M., Hughes G.M., Lavrichenko K., Devanna P.,
RA   Winkler S., Jermiin L.S., Skirmuntt E.C., Katzourakis A., Burkitt-Gray L.,
RA   Ray D.A., Sullivan K.A.M., Roscito J.G., Kirilenko B.M., Davalos L.M.,
RA   Corthals A.P., Power M.L., Jones G., Ransome R.D., Dechmann D.K.N.,
RA   Locatelli A.G., Puechmaille S.J., Fedrigo O., Jarvis E.D., Hiller M.,
RA   Vernes S.C., Myers E.W., Teeling E.C.;
RT   "Six reference-quality genomes reveal evolution of bat adaptations.";
RL   Nature 583:578-584(2020).
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KAF6377619.1}.
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DR   EMBL; JABWUV010000002; KAF6377619.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A7J7ZU59; -.
DR   VEuPathDB; HostDB:GeneID_118676132; -.
DR   Proteomes; UP000527355; Unassembled WGS sequence.
DR   GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR   GO; GO:0031012; C:extracellular matrix; IEA:TreeGrafter.
DR   GO; GO:0005615; C:extracellular space; IEA:TreeGrafter.
DR   GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; IEA:TreeGrafter.
DR   GO; GO:0032836; P:glomerular basement membrane development; IEA:TreeGrafter.
DR   CDD; cd00247; Endostatin-like; 1.
DR   FunFam; 3.10.100.10:FF:000008; collagen alpha-1(XVIII) chain isoform X1; 1.
DR   FunFam; 3.40.1620.70:FF:000003; Collagen type XVIII alpha 1; 1.
DR   Gene3D; 3.40.1620.70; -; 1.
DR   Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR008160; Collagen.
DR   InterPro; IPR050149; Collagen_superfamily.
DR   InterPro; IPR010515; Collagenase_NC10/endostatin.
DR   InterPro; IPR016187; CTDL_fold.
DR   InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR   PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR   PANTHER; PTHR24023:SF714; COLLAGEN ALPHA-4(IV) CHAIN; 1.
DR   Pfam; PF01391; Collagen; 1.
DR   Pfam; PF20010; Collagen_trimer; 1.
DR   Pfam; PF06482; Endostatin; 1.
DR   SUPFAM; SSF56436; C-type lectin-like; 1.
PE   4: Predicted;
KW   Collagen {ECO:0000256|ARBA:ARBA00023119, ECO:0000313|EMBL:KAF6377619.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000527355}.
FT   DOMAIN          264..312
FT                   /note="Collagen type XV/XVIII trimerization"
FT                   /evidence="ECO:0000259|Pfam:PF20010"
FT   DOMAIN          400..569
FT                   /note="Collagenase NC10/endostatin"
FT                   /evidence="ECO:0000259|Pfam:PF06482"
FT   REGION          1..263
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          366..386
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        73..88
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        143..163
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        164..174
FT                   /note="Gly residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        175..187
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        217..233
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        243..255
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   573 AA;  60115 MW;  819A4A22790D8BDE CRC64;
     MVFSPDGRVL PPAQKGAKGE PGFRGPPGPY GRPGHKGEIG FPGRPGRPGM NGFKGEKGEP
     GDASVGFGAR GPPGLPGPPG PPGPPGLPGN PVYDTNAFVE SGPVGPPGLP GHQGPSGPKG
     DKGEVGPPGP PGQFPFDFLQ LEAELKGDKG DRGDTGQKGE RGEPGGGGFF GSGVPGPPGP
     PGYPGIPGPK GESIRGQPGP PGPQGPPGIG YEGRQGPPGP PGPPGPPGPP SFPGPYRQTI
     SIPGPPGPPG PPGPPGTLGT SSGVRIWPTY QTMLDKVPEV PEGWLIFVAD REELYVRVRN
     GIRKVLLEAR TPLPRGTDNE VAALQPPLVQ LHEGNPHPRW ELPPSTSRPW RADDILVRPP
     RLLDPQPYPG VPHHGSYVHS RPAHPTGAPA HTHHDFQPVL HLVALNGPQP GGLRGIRGAD
     LQCFQQARAA GLAGTFRAFL SSRLQDLYSI VRRADRATVP IVNLRDEELF PNWEALFSGS
     QGQLKPGARI FSFDGRDVLQ HPAWPQKSVW HGSDPSGRRL TESYCETWRT EATTATGQAS
     SMLTGRLLGQ KAVSCHNAFI VLCIENSFMT SSK
//
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