ID A0A7J8B6V9_ROUAE Unreviewed; 1292 AA.
AC A0A7J8B6V9;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 08-OCT-2025, entry version 17.
DE SubName: Full=Collagen type XVIII alpha 1 chain {ECO:0000313|EMBL:KAF6394458.1};
GN ORFNames=HJG63_003140 {ECO:0000313|EMBL:KAF6394458.1};
OS Rousettus aegyptiacus (Egyptian fruit bat) (Pteropus aegyptiacus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Yinpterochiroptera; Pteropodoidea;
OC Pteropodidae; Rousettinae; Rousettus.
OX NCBI_TaxID=9407 {ECO:0000313|EMBL:KAF6394458.1, ECO:0000313|Proteomes:UP000593571};
RN [1] {ECO:0000313|EMBL:KAF6394458.1, ECO:0000313|Proteomes:UP000593571}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRouAeg1 {ECO:0000313|EMBL:KAF6394458.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:KAF6394458.1};
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 -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
CC -!- SIMILARITY: Belongs to the multiplexin collagen family.
CC {ECO:0000256|ARBA:ARBA00061275}.
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:KAF6394458.1}.
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DR EMBL; JACASE010000020; KAF6394458.1; -; Genomic_DNA.
DR Proteomes; UP000593571; 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:0007155; P:cell adhesion; IEA:UniProtKB-KW.
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 FunFam; 2.60.120.200:FF:000039; Collagen XV alpha 1 chain; 1.
DR Gene3D; 2.60.120.200; -; 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; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR048287; TSPN-like_N.
DR InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR PANTHER; PTHR24023:SF1112; COL_CUTICLE_N DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR Pfam; PF01391; Collagen; 3.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 1.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE 3: Inferred from homology;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Collagen {ECO:0000256|ARBA:ARBA00023119, ECO:0000313|EMBL:KAF6394458.1};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydroxylation {ECO:0000256|ARBA:ARBA00023278};
KW Proteoglycan {ECO:0000256|ARBA:ARBA00022974};
KW Reference proteome {ECO:0000313|Proteomes:UP000593571};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..33
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 34..1292
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5029471833"
FT DOMAIN 41..229
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 231..983
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..321
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..382
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..426
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..465
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..508
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..571
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..616
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..626
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..660
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..675
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 685..700
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 761..773
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 794..807
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 864..882
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 894..906
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 916..925
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 936..952
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 962..974
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1292 AA; 130153 MW; 96460A786FF948FA CRC64;
MAPRWPWLQP PRRHLLDVLA PLVLLLGVRG ASAEPESAGT EVGLLQLLGE PLPQHVAQVD
DPDVGPAFVF GADSSGGQAA RAHLPSPFFR DFALLFHVRP AAEGPGVLLA VTDAAQAVVS
VGVKLSGVRD GHQDVQLLYT EPGAARTRVA ASFRLPAFAG QWTRLALSVG GDSAALFVDC
EELQRVPLAR SPQRLQLEPG AGLFVAQAGA ADPDRFQGAI AELRVRGDPQ VSPLHCLEDD
ADDDRDRASG DFGSGLQASP ELAGEEAGMS LQPGLPEAPP VTSPPLAGGS NSEDSRTEEI
EEETTASSLG AQTLPGSQTA ATGDGNVRSP EDSLEEDPAG PLVPGPDARL VPGPQGPPGP
PGKDGAPGRD GEPGDPGKDG RPGDTGPQGF PGTPGDVGPK GEKGDPGVGP RGPPGPQGPP
GPPGPPFSQD KLTFIDMEGS GFGGDLESLR GPRGFPGPPG PPGVPGLPGQ PGRFGANSSA
TPGPAGMPGV PGRDGQPGPP GPPGPPGSPG REGRPGEAGQ KGSLGKDGAP GLKGSRGDPG
PAGAPGENGL TGAPGPAGPP GPPGPPGPPG PGLAAGFDDM EGSGGPFWPT TRGAEGLQGP
PGQPGAKGDP GIAGPPGAKG GAGADGPPGF PGLPGREGVA GAQGPKGEKG TPGEKGDPGK
DGVGQPGPPG PPGVPGPVIY LSEQDGQPGF AGFPGPAGPK GDPGSGGQPG PPGMKGEKGE
PGMVYGPDGH GLAPAPKGAK GEPGPRGPLG PYGRPGHKGE IGFPGRPGRP GINGLKGEKG
EPGDASIGFG VRGPPGPPGP PGPPGVPGTP VYDSNAFVES GPPGPPGLPG HQGPSGPKGD
KGEVGPPGAP GQFPLDLFQL GAEMKGEKGD RGHAGQKGER GEPGAGGFFG SSIPGPPGPP
GYPGIPGPKG ESTPGQPGPP GPQGPPGIGY EGRQGPPGPP GPPGPPGPPS FPGPYRQTIS
VPGPPGPPGP PGPPGTMGTS SGVRIWPTYQ TMLDRVPELP EGWLIYVAER EELYVRVRHG
FRKVLLEART SLPRGTENEV AALQPPLVQL HEGNPHPRGE LPPSTARPWR ADDVLASPPR
WRDPQPYPGV PHYGSYVQPW PVRPTGTPAH PHQDFRPVLH LVALNGPQPG GLRGIRGADL
QCFQQARAAG LAGTFRAFLS SRLQDLHSIV RRADRAAVPV VNLRDEELFP SWGALFSGSE
AQLKPGARIL SFDGRDVLQH PAWPQKSVWH GSDPSGRRLT ESYCETWRTE AMTATGQASS
LLAGKLLEQK AASCHNAFIV LCIENSLTTA SK
//
