ID Q90689_CHICK Unreviewed; 390 AA.
AC Q90689;
DT 01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE SubName: Full=Type V collagen {ECO:0000313|EMBL:AAB41274.1};
DE Flags: Fragment;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031 {ECO:0000313|EMBL:AAB41274.1};
RN [1] {ECO:0000313|EMBL:AAB41274.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=White leghorn {ECO:0000313|EMBL:AAB41274.1};
RC TISSUE=Cornea {ECO:0000313|EMBL:AAB41274.1};
RX PubMed=8947562; DOI=10.1083/jcb.135.5.1415;
RA Marchant J.K., Hahn R.A., Linsenmayer T.F., Birk D.E.;
RT "Reduction of type V collagen using a dominant-negative strategy alters the
RT regulation of fibrillogenesis and results in the loss of corneal-specific
RT fibril morphology.";
RL J. Cell Biol. 135:1415-1426(1996).
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; U39621; AAB41274.1; -; mRNA.
DR RefSeq; NP_990121.2; NM_204790.2.
DR AlphaFoldDB; Q90689; -.
DR GeneID; 395568; -.
DR KEGG; gga:395568; -.
DR CTD; 1289; -.
DR VEuPathDB; HostDB:geneid_395568; -.
DR OrthoDB; 2970887at2759; -.
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; IPR008160; Collagen.
DR InterPro; IPR000885; Fib_collagen_C.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF387; COLLAGEN ALPHA-1(V) CHAIN; 1.
DR Pfam; PF01410; COLFI; 1.
DR Pfam; PF01391; Collagen; 3.
DR SMART; SM00038; COLFI; 1.
DR PROSITE; PS51461; NC1_FIB; 1.
PE 2: Evidence at transcript level;
KW Collagen {ECO:0000313|EMBL:AAB41274.1};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Secreted {ECO:0000256|ARBA:ARBA00022530}.
FT DOMAIN 161..389
FT /note="Fibrillar collagen NC1"
FT /evidence="ECO:0000259|PROSITE:PS51461"
FT REGION 1..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..91
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..124
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAB41274.1"
SQ SEQUENCE 390 AA; 41099 MW; FC072DD294E87610 CRC64;
ALPGSPGPDG PPGPLGPPGL PGLKGDSGPK GEKGHPGLIG LIGPPGEQGE KGDRGLPGPQ
GSAGPKGEQG ITGPSGPIGP PGPPGLPGPP GPKGAKGSSG PTGPKGESGL PGPPGPPGPP
GEVIQPLPIQ SSKRTRRNID ASQLVDDGNA DNYMDYADGM EEIFGSLNSL KLEIEQMKHP
LGTQHNPART CKDLQLCHPD FPDGEYWVDP NQGCSRDSFK VYCNFTAGGE TCIFPDKKSE
GARITSWPKE NPGSWFSEFK RGKLLSYVDS DGNPIGVVQM TFLRLLSASA HQNITYNCYQ
SVAWHDATTD SYDKAIRFLG SNDEEMSYDN NPYIRAAFDG CAAKKGYQKT VLEINTPKVE
QVPIVDIMFN DFGEASQKFG FEVGPACFMG
//