ID G1RCL9_NOMLE Unreviewed; 1386 AA.
AC G1RCL9;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 3.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=Collagen type I alpha 1 chain {ECO:0000313|Ensembl:ENSNLEP00000010968.3};
GN Name=COL1A1 {ECO:0000313|Ensembl:ENSNLEP00000010968.3};
OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Nomascus.
OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000010968.3, ECO:0000313|Proteomes:UP000001073};
RN [1] {ECO:0000313|Ensembl:ENSNLEP00000010968.3, ECO:0000313|Proteomes:UP000001073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Gibbon Genome Sequencing Consortium;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSNLEP00000010968.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Type I collagen is a member of group I collagen (fibrillar
CC forming collagen). {ECO:0000256|ARBA:ARBA00003647}.
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; ADFV01128872; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01128873; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01128874; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 61853.ENSNLEP00000010968; -.
DR Ensembl; ENSNLET00000011502.2; ENSNLEP00000010968.3; ENSNLEG00000008996.2.
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00940000156584; -.
DR HOGENOM; CLU_001074_20_0_1; -.
DR InParanoid; G1RCL9; -.
DR OMA; YYDRDVW; -.
DR Proteomes; UP000001073; Chromosome 14.
DR GO; GO:0005584; C:collagen type I trimer; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0048407; F:platelet-derived growth factor binding; IEA:Ensembl.
DR GO; GO:0002020; F:protease binding; IEA:Ensembl.
DR GO; GO:0001568; P:blood vessel development; IEA:Ensembl.
DR GO; GO:0060346; P:bone trabecula formation; IEA:Ensembl.
DR GO; GO:0060351; P:cartilage development involved in endochondral bone morphogenesis; IEA:Ensembl.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; IEA:Ensembl.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
DR GO; GO:0032964; P:collagen biosynthetic process; IEA:Ensembl.
DR GO; GO:0030199; P:collagen fibril organization; IEA:Ensembl.
DR GO; GO:0048706; P:embryonic skeletal system development; IEA:Ensembl.
DR GO; GO:0001958; P:endochondral ossification; IEA:Ensembl.
DR GO; GO:0060325; P:face morphogenesis; IEA:Ensembl.
DR GO; GO:0001957; P:intramembranous ossification; IEA:Ensembl.
DR GO; GO:0010812; P:negative regulation of cell-substrate adhesion; IEA:Ensembl.
DR GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl.
DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IEA:Ensembl.
DR GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IEA:Ensembl.
DR GO; GO:0034504; P:protein localization to nucleus; IEA:Ensembl.
DR GO; GO:0015031; P:protein transport; IEA:Ensembl.
DR GO; GO:0007605; P:sensory perception of sound; IEA:Ensembl.
DR GO; GO:0043589; P:skin morphogenesis; IEA:Ensembl.
DR GO; GO:0034505; P:tooth mineralization; IEA:Ensembl.
DR GO; GO:0007601; P:visual perception; IEA:Ensembl.
DR Gene3D; 2.60.120.1000; -; 1.
DR Gene3D; 1.20.5.320; 6-Phosphogluconate Dehydrogenase, domain 3; 1.
DR Gene3D; 2.10.70.10; Complement Module, domain 1; 1.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR000885; Fib_collagen_C.
DR InterPro; IPR001007; VWF_dom.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF1108; ENDOSTATIN DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01410; COLFI; 1.
DR Pfam; PF01391; Collagen; 14.
DR Pfam; PF00093; VWC; 1.
DR SMART; SM00038; COLFI; 1.
DR SMART; SM00214; VWC; 1.
DR SUPFAM; SSF57603; FnI-like domain; 1.
DR PROSITE; PS51461; NC1_FIB; 1.
PE 4: Predicted;
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000001073};
KW Secreted {ECO:0000256|ARBA:ARBA00022530}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1386
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014191018"
FT DOMAIN 1156..1386
FT /note="Fibrillar collagen NC1"
FT /evidence="ECO:0000259|PROSITE:PS51461"
FT REGION 81..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..1140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..138
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..375
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..514
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 830..844
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1103..1122
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1386 AA; 133744 MW; F132E63582DF732A CRC64;
MFSFVDLRLL LLLAATALLT HGQEEGQVEG QDEDIPPITC VQNGLRYHDR DVWKPEPCRI
CVCDNGKVLC DDQTLALTRV SSPLESPTDQ ETTGVEGPKG DTGPRGPRGP AGPPGRDGIP
GQPGLPGPPG PPGPPGPPVS SIIGAVFCLS IHCPDPDFSC FPWAVVGRQG HDGLFSPSQG
EAGKPGRPGE RGPPGPQVSR RLRLNLGFTA LGLHLGGFSG LDGAKGDAGP AGPKGEPGSP
GENGAPGQMG PRGLPGERGR PGAPGPAGAR GNDGATGAAG PPVSVACNVG FPRVGEAGPQ
GPRGSEGPQG VRGEPGPPGP AGAAGPAGNP GADGQPGAKG ANGAPGIAGA PGFPGARGPS
GPQGPGGPPG PKGNSGEPGA PGSKGDTGAK GEPVSLPATL LAAQPTLPWE PPEGNPERKR
SSWSPGGVPG GPGSRGFPGA DGVAGPKGPA GERGSPGPAG PKGSPGEAGR PGEAGLPGAK
GLTGSPGSPG PDGKTGPPGP AGQDGRPGPP GPPGARGQAG VMGFPGPKGA AGEPGKAGER
GVPGPPGAVG PAGKDGEAGA QGPPGPAGPA GERGEQGPAG SPGFQGLPGP AGPPGEAGKP
GEQGVPGDLG APGPSGARGE RGFPGERGVQ GPPGPAGPRG ANGAPGNDGA KGDAGAPGAP
GSQGAPGLQG MPGERGAAGL PGPKGDRGDA GPKGADGSPG KDGVRGLTGP IGPPGPAGAP
GDKGETGPSG PAGPTGARGA PGDRGEPGPP GPAGFAGPPG ADGQPGAKGE PGDAGAKGDA
GPPGPAGPAG PPGPIGNVGA PGAKGARGSA GPPGATGFPG AAGRVGPPGP SGNAGPPGPP
GPAGKEGGKG PRGETGPAGR PGEVGPPGPP GPAGEKGSPG ADGPAGAPGT PGPQGIAGQR
GVVGLPGQRG ERGFPGLPGE PGKQGPSGAS GERGPPGPMG PPGLAGPPGE SGREGAPGAE
GSPGRDGLLA PRGGLILQPQ PQPPLAKRSC FPCSPQGPAG PAGPVGPVGA RGPAGPQGPR
GDKGETGEQG DRGIKGHRGF SGLQGPPGPP GSPGEQGPSG ASGPAGPRGP PGSAGAPGKD
GLNGLPGPIG PPGPRGRTGD AGPVGPPGPP GPPGPPGPPS AGFDFSFLPQ PPQEKAHDGG
RYYRADDANV VRDRDLEVDT TLKSLSQQIE NIRSPEGSRK NPARTCRDLK MCHSDWKSGE
YWIDPNQGCN LDAIKVFCNM ETGETCVYPT QPSVAQKNWY ISKNPKDKRH VWFGESMTDG
FQFEYGGQGS DPADVAIQLT FLRLMSTEAS QNITYHCKNS VAYMDQQTGN LKKALLLQGS
NEIEIRAEGN SRFTYSVTVD GCTSHTGAWG KTVIEYKTTK TSRLPIIDVA PLDVEFGFDV
GPVCFL
//
