ID L5JYK2_PTEAL Unreviewed; 1688 AA.
AC L5JYK2;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 28-JAN-2026, entry version 53.
DE SubName: Full=Collagen alpha-1(XVIII) chain {ECO:0000313|EMBL:ELK03591.1};
GN ORFNames=PAL_GLEAN10002957 {ECO:0000313|EMBL:ELK03591.1};
OS Pteropus alecto (Black flying fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Yinpterochiroptera; Pteropodoidea;
OC Pteropodidae; Pteropodinae; Pteropus.
OX NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK03591.1, ECO:0000313|Proteomes:UP000010552};
RN [1] {ECO:0000313|Proteomes:UP000010552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00090}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KB031079; ELK03591.1; -; Genomic_DNA.
DR FunCoup; L5JYK2; 81.
DR STRING; 9402.L5JYK2; -.
DR InParanoid; L5JYK2; -.
DR Proteomes; UP000010552; 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:0030198; P:extracellular matrix organization; IEA:TreeGrafter.
DR CDD; cd00110; LamG; 1.
DR FunFam; 1.10.2000.10:FF:000017; Alpha 1 type XVIII collagen; 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; 1.10.2000.10; Frizzled cysteine-rich domain; 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; IPR010363; DUF959_COL18_N.
DR InterPro; IPR020067; Frizzled_dom.
DR InterPro; IPR036790; Frizzled_dom_sf.
DR InterPro; IPR001791; Laminin_G.
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; PF06121; DUF959; 1.
DR Pfam; PF06482; Endostatin; 1.
DR Pfam; PF01392; Fz; 1.
DR SMART; SM00063; FRI; 1.
DR SMART; SM00282; LamG; 1.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF63501; Frizzled cysteine-rich domain; 1.
DR PROSITE; PS50038; FZ; 1.
PE 4: Predicted;
KW Collagen {ECO:0000256|ARBA:ARBA00023119, ECO:0000313|EMBL:ELK03591.1};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00090}; Reference proteome {ECO:0000313|Proteomes:UP000010552};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..1688
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003968649"
FT DOMAIN 337..454
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT REGION 37..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 126..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 277..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 675..1401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..65
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..96
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..153
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..215
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 759..773
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 819..835
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 852..861
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 864..878
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 908..918
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 976..988
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1003..1018
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1064..1073
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1093..1107
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1113..1122
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1211..1224
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1241..1250
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1283..1301
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1313..1325
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1335..1344
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1355..1371
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1381..1393
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 352..398
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 389..427
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
SQ SEQUENCE 1688 AA; 172086 MW; 10C105BA24E4F4E4 CRC64;
MAPQRSSRRG LWLLLLLTCG LAAARADMMD WLWSPSRAAE PPAGPPVPTT EDTTAAAPQA
DPTEQWTVPA GSELPRERLE AGQGEAPAAP RAPTASPDRR EENVAGVGAK ILSLATGIRS
FIQLWDDSTP TEGTSSAEAP APATPTDPLR TLPGPSSASQ DGGTPLWLSS GAPSPPDTQW
TGTGTRPVPT LLPPASGRPQ ALPSASRTSA GSALSSLPDG APPWGSRQSP GWPQDLDGEG
LSRVAARPRR QHRHPGILRL GPRLLRLVAG PPGVHAAPWA LRSSSPAKPS RLSRSPLTGD
GGAWDPHAAG PVGPGLANSS VLLWAEASTA HGQPGRPVPG RCLPLPPALL VCSRLGIGHA
WLPKHLPHAH AEQVPAASGA WGRLLETHCH RFLAWFLCLL LASPCGPGPP PALPPCRQFC
EALQDACWSH LDGDGLPVPC ASLPAQEDGR CVFLGPAAES VGAEVGLLQL LGEPPPQHVT
QVDDPDVGPA YVFGPDASGG QAARAHLPSP FFRDFSLLFY VRPATEGAGV LFAITDAAQA
VVSVGVKLSG VRDGHQHVQL LYTEPGTAQT RTAASFRLPA FTGQWTRLAL SVDGDTVALF
VDCEELQRVP LARSPQRLQL EPGAGLFVAQ AGAADPDSFQ GAIAELRVRG DPQVSPLHCL
EDDDDDDRDR GAIAELRVRG DPQVSPLHCL EDDDDDDRDR ASGDFGSGLQ GSPELAGEEV
GMSSQPGLPE APPATSPPLA GGSNSEDSRT EETEEETTAS SLGAQTLPGS HTVVTGDGNV
WSPGDSLEED PAGPVVQGPD ARLVPGPQGP PGPPGKDGAP GRDGEPGDPG KDGRPGDTGP
QGFPGTPGDV GPKGEKGDPR VGPRGPPGPQ GPPGPPGPSF RQDKLTFIDM EGSGFGGDLE
SLRGPRGFPG PPGPPGVPGL PGQPGRFGVN SSATPGPAGL PGVPGRDGHP GLPGPPVRPA
SVFPSGSTGN GGAEGAPGPK GSKGDPGPIG APGVNGLTGA PGPAGPPGPP GPPGPPGPGL
AAGFDDMEGS GGPFWPTARG ADGLQGPPGQ PGAKGDPGIM GPPGAKGGAG ADGPPGFPGL
PGREGAAGAQ GPKGEKGTRG EKGDPGKDGV GQPGPPGPPG IPGPIIYLSE QDGEKGEPGM
VYGPDGRGLA PAHKGAKGEP GPRGPPGPYG RPGHKGEIGF PGRPGRPGMN GFKGEKGEPG
DASVGFGVQG PPGPPGPPGP PGLPGTPXFA RSLQAFMESG PPGPPGPPGH QGPSGPKGDK
GEVGSPGAPG QFPLDLFQLG SEMKGEKGDR GHTGQKGERG EPGAGGFFGS SIPGPPGPPG
YPGIPGPKGE STPGQPGPPG PRGPPGVGYE GRQGPPGPPG PPGPPGPPSF PGPYRQTISV
PGPPGPPGPP GPPGTMGTAS GVRIWPTYQT MLDRVPELPE GWLVFVAEGE ELYVRVRDGF
RKVLLGARTP LPRGTDNEVA ALQPPLVQLH EGNPHPRGQL PPSTARPWRA DDVLASPPRW
RDPQPYPGVP HYSSYVQPWP ARPTGTPAHP HQDFRPVCFQ QARAAGLAGT FRAFLSSRLQ
DLHSIVRRAD RANVPVVNLR DEELFPSWGA LFSGSEAPLK PGARILSFDG RDVLQHPTWP
QKSVWHGSDP SGRRLTESYC ETWRTEAATA TGQASSLLAG KLLEQKAASC HNAFIVLCIE
NSLTTSSK
//
