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Database: UniProt
Entry: A0A7J7ZUU1_MYOMY
LinkDB: A0A7J7ZUU1_MYOMY
Original site: A0A7J7ZUU1_MYOMY 
ID   A0A7J7ZUU1_MYOMY        Unreviewed;       727 AA.
AC   A0A7J7ZUU1;
DT   07-APR-2021, integrated into UniProtKB/TrEMBL.
DT   07-APR-2021, sequence version 1.
DT   28-JAN-2026, entry version 15.
DE   SubName: Full=Collagen type XVIII alpha 1 chain {ECO:0000313|EMBL:KAF6377616.1};
GN   ORFNames=mMyoMyo1_003131 {ECO:0000313|EMBL:KAF6377616.1};
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:KAF6377616.1, ECO:0000313|Proteomes:UP000527355};
RN   [1] {ECO:0000313|EMBL:KAF6377616.1, ECO:0000313|Proteomes:UP000527355}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MMyoMyo1 {ECO:0000313|EMBL:KAF6377616.1};
RC   TISSUE=Flight muscle {ECO:0000313|EMBL:KAF6377616.1};
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:KAF6377616.1}.
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DR   EMBL; JABWUV010000002; KAF6377616.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A7J7ZUU1; -.
DR   VEuPathDB; HostDB:GeneID_118676132; -.
DR   Proteomes; UP000527355; Unassembled WGS sequence.
DR   GO; GO:0005594; C:collagen type IX trimer; 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:0030198; P:extracellular matrix organization; 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:SF1116; MACROPHAGE RECEPTOR WITH COLLAGENOUS STRUCTURE; 1.
DR   Pfam; PF01391; Collagen; 2.
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:KAF6377616.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000527355}.
FT   DOMAIN          418..466
FT                   /note="Collagen type XV/XVIII trimerization"
FT                   /evidence="ECO:0000259|Pfam:PF20010"
FT   DOMAIN          554..723
FT                   /note="Collagenase NC10/endostatin"
FT                   /evidence="ECO:0000259|Pfam:PF06482"
FT   REGION          1..100
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          115..417
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          520..540
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..37
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        67..81
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        87..96
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        227..242
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        297..317
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        318..328
FT                   /note="Gly residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        329..341
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        371..387
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        397..409
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   727 AA;  74581 MW;  597DBD190A223DDA CRC64;
     MEGSGGPFWL TARGADGLQG PPGKPGAKGD PGIAGPPGTK GEVGADGPPG FPGLPGKEGV
     AGAQGPKGEK GTQGEKGDPG KDGVGQPGPP GPPGLPGPVV YVSEEQDRAV SVTHGVKGQP
     GYAGLPGPAG PKGDTGVSGQ PGPPGPKGEK GEPGMVFSPD GRVLPPAQKG AKGEPGFRGP
     PGPYGRPGHK GEIGFPGRPG RPGMNGFKGE KGEPGDASVG FGARGPPGLP GPPGPPGPPG
     LPGNPVYDTN AFVESGPVGP PGLPGHQGPS GPKGDKGEVG PPGPPGQFPF DFLQLEAELK
     GDKGDRGDTG QKGERGEPGG GGFFGSGVPG PPGPPGYPGI PGPKGESIRG QPGPPGPQGP
     PGIGYEGRQG PPGPPGPPGP PGPPSFPGPY RQTISIPGPP GPPGPPGPPG TLGTSSGVRI
     WPTYQTMLDK VPEVPEGWLI FVADREELYV RVRNGIRKVL LEARTPLPRG TDNEVAALQP
     PLVQLHEGNP HPRWELPPST SRPWRADDIL VRPPRLLDPQ PYPGVPHHGS YVHSRPAHPT
     GAPAHTHHDF QPVLHLVALN GPQPGGLRGI RGADLQCFQQ ARAAGLAGTF RAFLSSRLQD
     LYSIVRRADR ATVPIVNLRD EELFPNWEAL FSGSQGQLKP GARIFSFDGR DVLQHPAWPQ
     KSVWHGSDPS GRRLTESYCE TWRTEATTAT GQASSMLTGR LLGQKAVSCH NAFIVLCIEN
     SFMTSSK
//
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