ID A6YLM2_CEREL Unreviewed; 205 AA.
AC A6YLM2;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Collagen type I alpha 1 {ECO:0000313|EMBL:ABR68236.1};
DE Flags: Fragment;
GN Name=COL1A1 {ECO:0000313|EMBL:ABR68236.1};
OS Cervus elaphus (Red deer).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Cervidae;
OC Cervinae; Cervus.
OX NCBI_TaxID=9860 {ECO:0000313|EMBL:ABR68236.1};
RN [1] {ECO:0000313|EMBL:ABR68236.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Bone {ECO:0000313|EMBL:ABR68236.1};
RA Borsy A., Orosz L.;
RT "Physiological versus pathological osteoporosis: Overlapping gene
RT expression pattern in deer and human.";
RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Type I collagen is a member of group I collagen (fibrillar
CC forming collagen). {ECO:0000256|ARBA:ARBA00003647}.
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DR EMBL; EF619481; ABR68236.1; -; mRNA.
DR AlphaFoldDB; A6YLM2; -.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IEA:InterPro.
DR Gene3D; 2.60.120.1000; -; 1.
DR InterPro; IPR000885; Fib_collagen_C.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF569; COLLAGEN ALPHA-1(I) CHAIN; 1.
DR Pfam; PF01410; COLFI; 1.
DR SMART; SM00038; COLFI; 1.
DR PROSITE; PS51461; NC1_FIB; 1.
PE 2: Evidence at transcript level;
KW Collagen {ECO:0000313|EMBL:ABR68236.1}.
FT DOMAIN 1..205
FT /note="Fibrillar collagen NC1"
FT /evidence="ECO:0000259|PROSITE:PS51461"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABR68236.1"
SQ SEQUENCE 205 AA; 22954 MW; 24F147C6DB09D043 CRC64;
RDLKMCHSDW KSGEYWIDPN QGCNLDAIKV FCNMETGETC VYPTQPSVAQ KNWYISKNPK
DKRHVWYGES MTGGFQFEYG GQGSDPADVA IQLTFLRLMS TEASQNITYH CKNSVAYMDQ
QTGNLKKALL LQGSNEIEIR AEGNSRFTYS VTYDGCTSHT GAWGKTVIEY KTTKTSRLPI
IDVAPLDVGA PDQEFGFDVG PVCFL
//
