ID M3YVG8_MUSPF Unreviewed; 1460 AA.
AC M3YVG8;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Collagen alpha-1(I) chain {ECO:0000313|RefSeq:XP_004764878.1};
DE SubName: Full=Collagen type I alpha 1 chain {ECO:0000313|Ensembl:ENSMPUP00000015328.1};
GN Name=COL1A1 {ECO:0000313|Ensembl:ENSMPUP00000015328.1,
GN ECO:0000313|RefSeq:XP_004764878.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000015328.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000015328.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_004764878.1}
RP IDENTIFICATION.
RC TISSUE=Brain {ECO:0000313|RefSeq:XP_004764878.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; AEYP01062188; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004764878.1; XM_004764821.3.
DR STRING; 9669.ENSMPUP00000015328; -.
DR Ensembl; ENSMPUT00000015567.1; ENSMPUP00000015328.1; ENSMPUG00000015438.1.
DR GeneID; 101686788; -.
DR KEGG; mpuf:101686788; -.
DR CTD; 1277; -.
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00940000156584; -.
DR HOGENOM; CLU_001074_2_3_1; -.
DR OMA; YYDRDVW; -.
DR OrthoDB; 2970887at2759; -.
DR Proteomes; UP000000715; Unplaced.
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; 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:SF58; COLLAGEN ALPHA-1(II) CHAIN; 1.
DR Pfam; PF01410; COLFI; 1.
DR Pfam; PF01391; Collagen; 12.
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.
DR PROSITE; PS01208; VWFC_1; 1.
DR PROSITE; PS50184; VWFC_2; 1.
PE 4: Predicted;
KW Collagen {ECO:0000313|RefSeq:XP_004764878.1};
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:UP000000715};
KW Secreted {ECO:0000256|ARBA:ARBA00022530}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1460
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5041199267"
FT DOMAIN 34..92
FT /note="VWFC"
FT /evidence="ECO:0000259|PROSITE:PS50184"
FT DOMAIN 1225..1460
FT /note="Fibrillar collagen NC1"
FT /evidence="ECO:0000259|PROSITE:PS51461"
FT REGION 96..1213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..152
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..222
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..429
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..568
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 838..852
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 884..898
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1172..1191
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1460 AA; 138705 MW; 6D7614A7F7245A69 CRC64;
MFSFVDLRLL LLLAATALLT HGQEEGQEED IPPVTCVQNG LRYYDRDVWK PEACRICVCD
NGNVLCDDVI CDETKNCPGA QVPPGECCPV CPDGEASPTD QETAGVEGPK GDTGPRGPRG
PAGPPGRDGI PGQPGLPGPP GPPGPPGPPG LGGNFAPQMS YGYDEKSTGG ISVPGPMGPS
GPRGLPGPPG APGPQGFQGP PGEPGEPGAS GPMGPRGPPG PPGKNGDDGE AGKPGRPGER
GPPGPQGARG LPGTAGLPGM KGHRGFSGLD GAKGDAGPAG PKGEPGSPGE NGAPGQMGPR
GLPGERGRPG APGPAGARGN DGATGAAGPP GPTGPAGPPG FPGAVGAKGE AGPQGARGSE
GPQGVRGEPG PPGPAGAAGP AGNPGADGQP GAKGANGAPG IAGAPGFPGA RGPSGPQGPS
GPPGPKGNSG EPGAPGNKGD TGAKGEPGPT GIQGPPGPAG EEGKRGARGE PGPTGLPGPP
GERGGPGSRG FPGADGVAGP KGPAGERGSP GPAGPKGSPG EAGRPGEAGL PGAKGLTGSP
GSPGPDGKTG PPGPAGQDGR PGPPGPPGAR GQAGVMGFPG PKGAAGEPGK AGERGVPGPP
GAVGPAGKDG EAGAQGAPGP AGPAGERGEQ GPAGSPGFQG LPGPAGPPGE AGKPGEQGVP
GDLGAPGPSG ARGERGFPGE RGVQGPPGPA GPRGANGAPG NDGAKGDAGA PGAPGSQGAP
GLQGMPGERG AAGLPGPKGD RGDAGPKGAD GSPGKDGVRG LTGPIGPPGP AGAPGDKGEA
GPSGPAGPTG ARGAPGDRGE PGPPGPAGFA GPPGADGQPG AKGEPGDAGA KGDAGPPGPA
GPTGPPGPIG NVGAPGPKGA RGSAGPPGAT GFPGAAGRVG PPGPSGNAGP PGPPGPAGKE
GGKGPRGETG PAGRPGEVGP PGPPGPAGEK GSPGADGPAG APGTPGPQGI AGQRGVVGLP
GQRGERGFPG LPGPSGEPGK QGPSGASGER GPPGPMGPPG LAGPPGESGR EGSPGAEGSP
GRDGSPGPKG DRGETGPAGP PGAPGAPGAP GPVGPAGKSG DRGETGPAGP AGPIGPVGAR
GPTGPQGPRG DKGETGEQGD RGIKGHRGFS GLQGPPGPPG SPGEQGPSGA SGPAGPRGPP
GSAGSPGKDG LNGLPGPIGP PGPRGRTGDA GPVGPPGPPG PPGPPGPPSG GFDFSFLPQP
PQEKAHDGGR YYRADDANVV RDRDLEVDTT LKSLSQQIEN IRSPEGSRKN PARTCRDLKM
CHSDWKSGEY WIDPNQGCNL DAIKVFCNME TGETCVYPTQ PQVAQKNWYI SKNPKEKRHV
WYGESMTDGF QFEYGGQGSD PADVAIQLTF LRLMSTEASQ NITYHCKNSV AYMDQQTGNL
KKALLLQGSN EIEIRAEGNS RFTYSVTYDG CTSHTGAWGK TVIEYKTTKT SRLPIIDVAP
LDVGAPDQEF GMDIGPVCFL
//
