ID A0A091NLL3_APAVI Unreviewed; 1624 AA.
AC A0A091NLL3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Collagen alpha-1(IV) chain {ECO:0000313|EMBL:KFP89804.1};
DE Flags: Fragment;
GN ORFNames=N311_01033 {ECO:0000313|EMBL:KFP89804.1};
OS Apaloderma vittatum (Bar-tailed trogon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Trogoniformes; Trogonidae; Apaloderma.
OX NCBI_TaxID=57397 {ECO:0000313|EMBL:KFP89804.1, ECO:0000313|Proteomes:UP000054244};
RN [1] {ECO:0000313|EMBL:KFP89804.1, ECO:0000313|Proteomes:UP000054244}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N311 {ECO:0000313|EMBL:KFP89804.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Type IV collagen is the major structural component of
CC glomerular basement membranes (GBM), forming a 'chicken-wire' meshwork
CC together with laminins, proteoglycans and entactin/nidogen.
CC {ECO:0000256|ARBA:ARBA00003696}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004370}.
CC Secreted, extracellular space, extracellular matrix, basement membrane
CC {ECO:0000256|ARBA:ARBA00004302}.
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DR EMBL; KL385640; KFP89804.1; -; Genomic_DNA.
DR Proteomes; UP000054244; 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:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IEA:InterPro.
DR Gene3D; 2.170.240.10; Collagen IV, non-collagenous; 1.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR001442; Collagen_IV_NC.
DR InterPro; IPR036954; Collagen_IV_NC_sf.
DR InterPro; IPR016187; CTDL_fold.
DR PANTHER; PTHR24023:SF1019; COLLAGEN; 1.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR Pfam; PF01413; C4; 2.
DR Pfam; PF01391; Collagen; 14.
DR SMART; SM00111; C4; 2.
DR SUPFAM; SSF56436; C-type lectin-like; 2.
DR PROSITE; PS51403; NC1_IV; 1.
PE 4: Predicted;
KW Basement membrane {ECO:0000256|ARBA:ARBA00022869};
KW Collagen {ECO:0000256|ARBA:ARBA00023119, ECO:0000313|EMBL:KFP89804.1};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Reference proteome {ECO:0000313|Proteomes:UP000054244};
KW Secreted {ECO:0000256|ARBA:ARBA00022530}.
FT DOMAIN 1400..1624
FT /note="Collagen IV NC1"
FT /evidence="ECO:0000259|PROSITE:PS51403"
FT REGION 1..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 119..1393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..163
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..216
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..251
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..384
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..621
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 698..712
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 758..778
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 907..933
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 945..959
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1200..1214
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1370..1389
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP89804.1"
FT NON_TER 1624
FT /evidence="ECO:0000313|EMBL:KFP89804.1"
SQ SEQUENCE 1624 AA; 156929 MW; BBD0B44CF8680D62 CRC64;
QGERGLPGLQ GVIGFPGMQG PEGHPGPPGL KGDTGEPGLP GTKGTRGPPG VSGFPGNPGL
PVHGPPGPPG IPGCNGTKGE RGPVGPPGLP GLTGSIGPPG PPGMKGDPGE VIGLLPPSLL
KGDKGFPGQP GLPGPPGAPG FQGTMGPQGP PGEPGPPGPP GLPGEKGYMG LGFQGPKGEK
GEQGVRGPPG PPGPAPHMKE KGTEIIRGEK GDPGEKGEQG VPGLPGSGFK GEKGEPGKPG
PRGKPGKDGE PGPKGDPGLP GGFGIPGRPG EPGVKGDKGE RGFPGLPGRV IDGPVDTFGE
KGEPGVSGLP GLKGQKGEKG FPGIQGVPGL PGRPLPDRVG SPGVPGQRGE KGEKGSPGFS
LPGPPGRDGF PGPPGLPGPP GPPGVTDGID QCQQGEPGAP GSPGLPGRDG FPGEMGEKGD
KGQSCALCDK VGPPGLPGPQ GPPGPSGFPG QSGFKGDRGL PGLDGLPGVP GPPGTPGLMG
SPGAKGDPGD FTYDSILKGE KGEPGFPGQA GIPGREGRPG KDGLPGPQGP KGAAGTPGLK
GERGPPGQPG FPGVRGERGF PGPPGIGVAG LPGDKGDRGF AGTPGLPGLP GAKGEAGRTV
PLPGPPGADG LPGPPGFPGP QGDKGNPGLP GRPGLPGEKG AVGQPGIGFP GPPGPKGFQG
QPGSPGLPGN PGTPGLDGLP GVPGLQGQKG EPGVGLPGPK GLPGPPGPAG IPGEKGSPGL
PGLRGEQGFP GIPGQQGFRG DPGLPGLQGL QGPPGAPGMG PRGTPGPAGQ PGPQGPPGFP
GIKGERGFPG IPGLDMPGPK GDKGSQGQPG VPGSVGLPGL PGPQGATGEK GSAGPKGEMG
VMGTPGLPGT PGPVGDRGFP GEKGSQGFKG VVGPQGDPGV KGDKGEAGLP GKPGTMDTMD
MVSLKGQKGD QGEKGDHGAT GEKGLRGEYG EPGRDGEPGT PGQPGPKGDQ GPPGYPGDPG
IPGQKGSVGA MGLPGTPGEK GLPGVPGSPG TPGFPGQKGE KGDKGAPGFP GIGFPGSPGE
KGEPGRTGSP GLSGDKGEKG SAGIPGMPGA PGPKGSPGMA GFPGNPGPHG EKGEKGLPGL
SGIPGLKGEP GEPGVPGPAG SVGQKGERGY DGIPGPAGAK GEQGFPGRGL PGFPGAKGDK
GAKGEVGFPG SPGSPGIPGL KGEPGYAGPP GPKGSPGLPG LPGSAIEGPK GDRGPQGQPG
LPGLPGPTGP PGPPGLKGAK GEQGSNGWPG TPGGPGVKGD PGFQGLPGSP GLPGDIGQKG
DLGPPGVPGV PGPKGSSGFP GLKGERGDQG LPGSKGLQGP PGPPGAFQLV KGDPGLPGPV
GPVGLKGFPG LPGPKGQQGV TGPSGVPGPP GSPGFDGRPG QKGEVGPYGP PGPRGFPGPP
GPEGLPGAMG PPGAPSVAHG FLVTRHSQTI EEPLCPIGTR LIYHGYSLLY VQGNERAHGQ
DLGTAGSCLR KFSTMPFLFC NINNVCNFAS RNDYSYWLST PEPMPMNMAP ITGDNIRPFI
SRCSVCEAPA MVIAVHSQTI QIPPCPEGWS SLWIGYSFVM HTSAGAEGSG QALASPGSCL
EEFRSAPFIE CHGRGTCNYY ANAYSFWLAT IERNEMFKKP TPSTLKAGDL RSNVSRCQVC
MRKT
//
