ID H0WS67_OTOGA Unreviewed; 1469 AA.
AC H0WS67;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Collagen type II alpha 1 chain {ECO:0000313|Ensembl:ENSOGAP00000004915.2};
GN Name=COL2A1 {ECO:0000313|Ensembl:ENSOGAP00000004915.2};
OS Otolemur garnettii (Small-eared galago) (Garnett's greater bushbaby).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lorisiformes;
OC Galagidae; Otolemur.
OX NCBI_TaxID=30611 {ECO:0000313|Ensembl:ENSOGAP00000004915.2, ECO:0000313|Proteomes:UP000005225};
RN [1] {ECO:0000313|Proteomes:UP000005225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K., Jaffe D.B.,
RA Gnerre S., MacCallum I., Przybylski D., Ribeiro F.J., Burton J.N.,
RA Walker B.J., Sharpe T., Hall G.;
RT "Version 3 of the genome sequence of Otolemur garnettii (Bushbaby).";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSOGAP00000004915.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; AAQR03104217; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 30611.ENSOGAP00000004915; -.
DR Ensembl; ENSOGAT00000005497.2; ENSOGAP00000004915.2; ENSOGAG00000005487.2.
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00940000155224; -.
DR HOGENOM; CLU_001074_2_3_1; -.
DR InParanoid; H0WS67; -.
DR OMA; HIRMGET; -.
DR TreeFam; TF344135; -.
DR Proteomes; UP000005225; Unassembled WGS sequence.
DR GO; GO:0005604; C:basement membrane; IEA:Ensembl.
DR GO; GO:0005585; C:collagen type II 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:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042289; F:MHC class II protein binding; IEA:Ensembl.
DR GO; GO:0048407; F:platelet-derived growth factor binding; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0043394; F:proteoglycan binding; IEA:Ensembl.
DR GO; GO:0097065; P:anterior head development; IEA:Ensembl.
DR GO; GO:0001502; P:cartilage condensation; IEA:Ensembl.
DR GO; GO:0060351; P:cartilage development involved in endochondral bone morphogenesis; IEA:Ensembl.
DR GO; GO:0071773; P:cellular response to BMP stimulus; IEA:Ensembl.
DR GO; GO:0007417; P:central nervous system development; IEA:Ensembl.
DR GO; GO:0002062; P:chondrocyte differentiation; IEA:Ensembl.
DR GO; GO:0030199; P:collagen fibril organization; IEA:Ensembl.
DR GO; GO:0060272; P:embryonic skeletal joint morphogenesis; IEA:Ensembl.
DR GO; GO:0001958; P:endochondral ossification; IEA:Ensembl.
DR GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl.
DR GO; GO:0003007; P:heart morphogenesis; IEA:Ensembl.
DR GO; GO:0042472; P:inner ear morphogenesis; IEA:Ensembl.
DR GO; GO:0060174; P:limb bud formation; IEA:Ensembl.
DR GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl.
DR GO; GO:0030903; P:notochord development; IEA:Ensembl.
DR GO; GO:0071599; P:otic vesicle development; IEA:Ensembl.
DR GO; GO:0006029; P:proteoglycan metabolic process; IEA:Ensembl.
DR GO; GO:0010468; P:regulation of gene expression; IEA:Ensembl.
DR GO; GO:0060021; P:roof of mouth development; IEA:Ensembl.
DR GO; GO:0007605; P:sensory perception of sound; IEA:Ensembl.
DR GO; GO:0001894; P:tissue homeostasis; 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; 6.
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:0000256|ARBA:ARBA00023119};
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:UP000005225};
KW Secreted {ECO:0000256|ARBA:ARBA00022530}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1469
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003543890"
FT DOMAIN 32..90
FT /note="VWFC"
FT /evidence="ECO:0000259|PROSITE:PS50184"
FT DOMAIN 1254..1469
FT /note="Fibrillar collagen NC1"
FT /evidence="ECO:0000259|PROSITE:PS51461"
FT REGION 97..1252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..150
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..175
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..252
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..366
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..447
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 911..925
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1201..1218
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1469 AA; 140141 MW; 2CD4214B749D9C94 CRC64;
MIRLGAPQKL VLLTLLVAAV LRCQSQDVQE AGSCVQDGQR YNDKDVWKPE ACQICVCDTG
TVLCDDIICE DVKDCLSPEI PFGECCPICP TDLATASGWP PGPKGQKGEP GDIKDIVGPK
GPPGPQGPAG EQGPRGDRGD KGEKGAPGPR GRDGEPGTPG NPGPPGPPGP PGPPGLGGNF
AAQMAGGFDE KAGGAQMGVM QGPMGPMGPR GPPGPAGSPG PQGFQGNPGE PGEPGVSGPM
GPRGPPGPPG KPGDDGEAGK PGKSGERGPP GPQGARGFPG TPGLPGVKGH RGYPGLDGAK
GEAGAPGVKG ESGSPGENGS PGPMGPRGLP GERGRTGPAG AAGARGNDGQ PGPAGPPGPV
GPAGGPGFPG APGAKGEAGP TGARGPEGAQ GPRGEPGTPG SPGPAGASGN PGTDGIPGAK
GSAGAPGIAG APGFPGPRGP PGPQGATGPL GPKGQTGEPG IAGFKGEQGP KGEPGPAGPQ
GAPGPAGEEG KRGARGEPGG AGPVGPPGER GAPGNRGFPG QDGLAGPKGA PGERGPVGLA
GPKGANGDPG RPGEPGLPGA RGLTGRPGDA GPQGKVGPSG APGEDGRPGP PGPQGARGQP
GVMGFPGPKG ANGEPGKAGE KGLPGAPGLR GLPGKDGETG AAGPPGPAGP AGERGEQGAP
GPSGFQGLPG PPGPPGEGGK AGDQGVPGEA GAPGLVGPRG ERGFPGERGS PGAQGLQGPR
GLPGTPGTDG PKGASGPVGP TGAQGPPGLQ GMPGERGAAG IAGPKGDRGD VGEKGPEGAP
GKDGGRGLTG PIGPPGPAGA NGEKGEVGPP GPAGSAGARG APGERGETGP PGPAGFAGPP
GADGQPGAKG EQGEAGQKGD AGAPGPQGPS GAPGPQGPTG VTGPKGSRGA QGPPGATGFP
GAAGRVGPPG SNGNPGPPGP PGPSGKDGPK GSRGDSGPAG RAGDPGLQGP AGPPGEKGEP
GDEGPSGADG PPGPQGLAGQ RGIVGLPGQR GERGFPGLPG PSGEPGKQGA PGASGDRGPP
GPVGPPGLTG PAGEPGREGS PGADGPPGRD GAAGVKGDRG ETGALGAPGA PGPPGSPGPA
GPTGKQGDRG EAGAQGPMGP SGPAGARGLP GPQGPRGDKG ETGEAGERGL KGHRGFTGLQ
GLPGPPGPSG DQGASGPAGP SGPRGPPGPV GPSGKDGANG IPGPIGPPGP RGRSGETGPA
GPPGNPGPPG PPGPPGPGID MSAFAGLGQR EKGPDPLQYM RADQPAGSLR QHDAEVDATL
KSLNNQIESI RSPEGSRKNP ARTCRDLKLC HPEWKSGDYW IDPNQGCTLD AMKVFCNMET
GETCVYPNPA SVPKKNWWSS KSKEKKHIWF GETINGGFHF SYGDDNLAPN TASIQMTFLR
LLSTEGSQNI TYHCKNSIAY LDEAAGNLKK ALLIQGSNDV EIRAEGNSRF TYTTLKDGCT
KHTGKWDKTV IEYRSQKTSR LPILDFSPL
//
