ID A0A3M0KYV4_HIRRU Unreviewed; 1540 AA.
AC A0A3M0KYV4;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 28-JAN-2026, entry version 21.
DE RecName: Full=Collagen alpha-1(XVIII) chain {ECO:0000256|ARBA:ARBA00069367};
GN ORFNames=DUI87_04206 {ECO:0000313|EMBL:RMC18323.1};
OS Hirundo rustica rustica.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Passeriformes; Sylvioidea; Hirundinidae; Hirundo.
OX NCBI_TaxID=333673 {ECO:0000313|EMBL:RMC18323.1, ECO:0000313|Proteomes:UP000269221};
RN [1] {ECO:0000313|EMBL:RMC18323.1, ECO:0000313|Proteomes:UP000269221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Chelidonia {ECO:0000313|EMBL:RMC18323.1};
RC TISSUE=Blood {ECO:0000313|EMBL:RMC18323.1};
RA Formenti G., Chiara M., Poveda L., Francoijs K.-J., Bonisoli-Alquati A.,
RA Canova L., Gianfranceschi L., Horner D.S., Saino N.;
RT "A high quality draft genome assembly of the barn swallow (H. rustica
RT rustica).";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May regulate extracellular matrix-dependent motility and
CC morphogenesis of endothelial and non-endothelial cells; the function
CC requires homotrimerization and implicates MAPK signaling.
CC {ECO:0000256|ARBA:ARBA00053766}.
CC -!- FUNCTION: Probably plays a major role in determining the retinal
CC structure as well as in the closure of the neural tube.
CC {ECO:0000256|ARBA:ARBA00054383}.
CC -!- SUBUNIT: Forms homotrimers. Recombinant non-collagenous domain 1 has
CC stronger affinity to NID1, HSPG2 and laminin-1:NID1 complex and lower
CC affinity to FBLN1 and FBLN2 than endostatin.
CC {ECO:0000256|ARBA:ARBA00065165}.
CC -!- SUBUNIT: Monomeric. Interacts with KDR/VEGFR2. Interacts with the
CC ITGA5:ITGB1 complex. Interacts with NID1, HSPG2, laminin-1:NID1
CC complex, FBLN1 and FBLN2. {ECO:0000256|ARBA:ARBA00064471}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane {ECO:0000256|ARBA:ARBA00004302}.
CC -!- SIMILARITY: Belongs to the multiplexin collagen family.
CC {ECO:0000256|ARBA:ARBA00061275}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00090}.
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:RMC18323.1}.
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DR EMBL; QRBI01000096; RMC18323.1; -; Genomic_DNA.
DR STRING; 333673.A0A3M0KYV4; -.
DR OrthoDB; 5983381at2759; -.
DR Proteomes; UP000269221; Unassembled WGS sequence.
DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005615; C:extracellular space; IEA:TreeGrafter.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IEA:UniProtKB-ARBA.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0042127; P:regulation of cell population proliferation; IEA:UniProtKB-ARBA.
DR CDD; cd00247; Endostatin-like; 1.
DR FunFam; 1.10.2000.10:FF:000017; Alpha 1 type XVIII collagen; 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; 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; IPR020067; Frizzled_dom.
DR InterPro; IPR036790; Frizzled_dom_sf.
DR InterPro; IPR048287; TSPN-like_N.
DR InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF1082; COLLAGEN TRIPLE HELIX REPEAT; 1.
DR Pfam; PF01391; Collagen; 4.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 1.
DR Pfam; PF01392; Fz; 1.
DR SMART; SM00063; FRI; 1.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 2.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF63501; Frizzled cysteine-rich domain; 1.
DR PROSITE; PS50038; FZ; 1.
PE 3: Inferred from homology;
KW Basement membrane {ECO:0000256|ARBA:ARBA00022869};
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00090}; Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydroxylation {ECO:0000256|ARBA:ARBA00023278};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Proteoglycan {ECO:0000256|ARBA:ARBA00022974};
KW Reference proteome {ECO:0000313|Proteomes:UP000269221};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 313..431
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 41..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 192..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 628..1011
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1025..1049
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1061..1135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1178..1219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..212
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..645
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 724..740
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 769..783
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 811..823
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 858..867
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 885..894
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 902..914
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 980..994
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1000..1009
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1117..1130
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1182..1196
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1201..1210
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 328..374
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 365..403
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
SQ SEQUENCE 1540 AA; 161292 MW; EE84E876B9FD4A7A CRC64;
MSPAPGQQAA SSTTDDPQLL GTGTHKDPQL LRMRTTKDTQ FLGPVTSKDP QLLGTRTTEN
LQLLGSGSTE NPQLLRMEIT EDSPLLGSGT TEDLQLLGLG TTEDQQLLGM MSTTDLQLLE
TGHTEDPQLP GMGTTENPQL LAMRNTKDTQ LLRTVTTENP ELLGNTGNPL LLWTVTPEDP
ELLRTETPTA METQVSLQRP AGPQPGSAPF PFSPGDSTPE HAVPFQNPSA PPPRHLHGAS
PNTRHGTSHL GLALASRSGS QSPPWLDQRV DKGVDPPAAD NFVPVEFNLL TATMRLYGSG
GVGLASFFPG LTTGAGRCQP VPTHLPFCSV LGTSRVRLPN YLRHGSEEEI WAALHEWEGL
LESRCHRYLE WFLCLLLLPG CSPSVPVTPP PCQGFCEAVR DQCWTHLAGG RLPLPCDALP
EEDDGVSCVF INVSAESLSA EVSLLELIGD PPTEEIHRIY GPDNNPGYVF GPNANTGQVA
RYHLPSPFYR DFSLLFHIQP TTPRAGVLFA VTDSSQSIIY VGVKLSELQA GQQQIIFYYT
EPGSPSSYPA ATFTVPTLLN QWTRFAISVE EEEVVLYLDC EEHERVHFER SPDEMELEEG
SGLFVAQAGG ADPDKYQGVI ADLKLRGDPR AAERQCEEEE DDAEVSGDFG SGMEGGQQPS
SGKVEGEKGD LGVKGSAGFG YPGSKGQKGE PGDPGRPGTL SRHADGSVVE QVTGPPGPPG
KDGFPGRDGE PGDPGEDGKP GEMGPPGFPG MPGEPGLKGE KGDPGLGPRG PPGPPGPPGP
PGPSSKNDKL TFIDMEGSGF GSDLESLRGP RGPPGPPGPP GVPGLPGEPG RFGMNRTDLP
GPPGLPGRDG IPGPPGPAGD VGDLGLPGLP GPKGSKGEPG PAGPPGEMGL AGLPGPIGPQ
GQPGPPGPPG PPGPGYEAGF GDMEGSGLSF TPGPPGPAGP QGEVGSPGQP GLPGPKGDAG
MPGVDGRPGL EGFPGPQGPK GDKGSAGEKG ERGQDGVGLP GPPGPPGPPG QVITVSGEDK
PLVAFPGPEG RPGHAGFPGE KGEPGVIISP DGTVVTAKVK GEKGEPGLRG PMGPSGPPGR
AGMKGEIGFP GRPGRPGMNG LKGEKGDPAD VLGSRGPPGP PGPPGPPGPP GSIVYNNGNV
SITTVTMMDM LAIGPPDALV TSWLRLACQL PYDVSHFTTS LRGDKGDAGP KGEKGEPGST
PLYGPGVSGL PGPPGPQGYP GLPLRAMPTY QAMLSAAHEL PEGSLVFLTS RQELYVRLRG
GFRRVLLEEH NLIPSSALDN EVYDKPPTLH YASPQPRGPL HPLRNHVPPA TARPWHGDEV
VANQHRLPEK PLLHHQQELI NGYYVHHRPD PAPVAAHVHQ DFQPALHLVA LNTPQSGGMR
GIRGADFQCF QQARQVGLAG TFRAFLSSRL QDLYSIVRRA DRTDVPIVNL RDEVLFNNWE
ALFVGSGAPL RAGTRILSFD GRDVLQDAGW PQKNVWHGSD AKGRRLPESY CETWRTEERT
VTGQASSLAS GKLLEQAASS CQHAFIVLCI ENSFMTAAKK
//
