ID G3T4M5_LOXAF Unreviewed; 1354 AA.
AC G3T4M5;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE SubName: Full=Collagen type V alpha 1 chain {ECO:0000313|Ensembl:ENSLAFP00000008323.3};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000008323.3, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000008323.3, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000008323.3,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000008323.3}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000008323.3};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR STRING; 9785.ENSLAFP00000008323; -.
DR Ensembl; ENSLAFT00000009939.3; ENSLAFP00000008323.3; ENSLAFG00000009931.3.
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00940000159211; -.
DR HOGENOM; CLU_001074_2_3_1; -.
DR InParanoid; G3T4M5; -.
DR OMA; TQGFQGK; -.
DR TreeFam; TF344135; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
DR GO; GO:0005588; C:collagen type V trimer; IEA:Ensembl.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IEA:InterPro.
DR GO; GO:0008201; F:heparin binding; IEA:Ensembl.
DR GO; GO:0048407; F:platelet-derived growth factor binding; IEA:Ensembl.
DR GO; GO:0043394; F:proteoglycan binding; IEA:Ensembl.
DR GO; GO:0007155; P:cell adhesion; 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:0048592; P:eye morphogenesis; IEA:Ensembl.
DR GO; GO:0045112; P:integrin biosynthetic process; IEA:Ensembl.
DR GO; GO:1903225; P:negative regulation of endodermal cell differentiation; IEA:Ensembl.
DR GO; GO:0043588; P:skin development; IEA:Ensembl.
DR GO; GO:0035313; P:wound healing, spreading of epidermal cells; IEA:Ensembl.
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; 9.
DR SMART; SM00038; COLFI; 1.
DR PROSITE; PS51461; NC1_FIB; 1.
PE 4: Predicted;
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Reference proteome {ECO:0000313|Proteomes:UP000007646};
KW Secreted {ECO:0000256|ARBA:ARBA00022530}.
FT DOMAIN 1125..1353
FT /note="Fibrillar collagen NC1"
FT /evidence="ECO:0000259|PROSITE:PS51461"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 71..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 596..1110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..212
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..328
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..485
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 672..686
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 837..873
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 897..912
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 970..984
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1041..1056
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1072..1089
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1095..1110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1354 AA; 131531 MW; 96EFA1A47AA09936 CRC64;
LSSPPLSQGP PGRPGLPGAD GLPGPPGTML MLPPQFRFGG GGDAGSKGPM VSAQESQAQA
ILQQARLALR GPAGPMGLTG RPGPMGPPGS GGLKGEPGDM GPQGPRGVQG PPGPTGKPGR
RGRAGSDGAR GMPGQTGPKG DRGFDGLAGL PGEKGHRGDP GPSGPPGPPG EDGERGDDGE
VGPRGLPGEP GPRGLLGPKG PPGPPGPPGV TGMDGQPGPK GNVGPQGEPG PPGQQGNPGA
QGLPGPQGAI GPPGEKGPLG KPGLPGMPGA DGPPGHPGKE GPPGEKGGQG PPGPQGPIGY
PGPRGVKGAD GIRGLKGTKG EKGEDGFPGF KGDMGIKGDR GEIGPPGPRG EDGPEGPKGR
GGPNGDPGPL GPTGEKGRSK IRDFMHSSGV QAGQGSIGFP GFPGANGEKG GRGTPGKPGP
RGQRGPTGPR GERGPRGITG KPGPKGNSGG DGPAGPPGER GPNGPQGPTG FPGPKGPPGP
PGKDGLPGHP GQRGETGFQG KTGPPGPPGV VGPQGPTGET GPMGERGHPG PPGPPGEQGL
PGVAGKEGTK GDPGPAGIPG KDGPPGLRGF PGDRGLPGPV GALGLKGNLK AFETNRFLGP
TQGSPGERGP AGAAGPIGIP GRPGPQGPPG PAGEKGAPGE KGPQGPAGRD GLQGPVGLPG
PAGPVGAPGE DGDKGEIGEP GQKGSKGDKG EQGPPGPTGP QGPIGQPGPS GADGEPGPRG
QQGLFGQKGD EGPRGFPGPP GPVGLQGLPG PPGEKGETGD VGQMGPPGPP GPRGPSGAPG
ADGPQGPPGG IGNPGAVGEK GEPGEAGEPG LPGEGGPPGP KGERGEKGES GPSGAAGPPG
PKGPPGDDGP KGSPGPVGFP GDPGPPGEPG PAGQDGPPGD KGDDGEPGQT GSPGPTGEPG
PSGPPGKRGP PGPAGPEGRQ GEKGAKGEAG LEGPPGKTGP IGPQGAPGKP GPDGLRGIPG
PVGEQGLPGS PGPDGPPGPM GPPGLPGLKG DSGPKGEKGH PGLIGLIGPP GEQGEKGDRG
LPGPQGSSGP KGEQGITGPS GPIGPPGPPG LPGPPGPKGA KGSSGPTGPK GEAGQPGPPG
LPGPPGEVIQ PLPIQASRTR RNIDASQLMD EGNNENYMDY ADGMEEIFGS LNSLKLEIEQ
MKRPLGTQQN PARTCKDLQL CHPDFPDGEY WVDPNQGCSR DSFKVYCNFT AGGSTCIFPD
KKSEGARITS WPKENPGSWF SEFKRGKLLS YVDAEGNPVG VVQMTFLRLL SASAHQNVTY
NCYQSVAWQD AATGSYDKAI RFLGSNDEEM SYDNNPYIRA LVDGCATRKG YQKTVLEIDT
PKVEQVPLVD IMFNDFGEAS QKFGFEVGPA CFMG
//
