ID M7BTL3_CHEMY Unreviewed; 1037 AA.
AC M7BTL3;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE SubName: Full=Collagen alpha-1(IV) chain {ECO:0000313|EMBL:EMP35428.1};
DE Flags: Fragment;
GN ORFNames=UY3_07391 {ECO:0000313|EMBL:EMP35428.1};
OS Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP35428.1, ECO:0000313|Proteomes:UP000031443};
RN [1] {ECO:0000313|Proteomes:UP000031443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
CC -!- FUNCTION: Type IV collagen is the major structural component of
CC glomerular basement membranes (GBM), forming a 'chicken-wire' meshwork
CC together with laminins, proteoglycans and entactin/nidogen.
CC {ECO:0000256|ARBA:ARBA00003696}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004370}.
CC Secreted, extracellular space, extracellular matrix, basement membrane
CC {ECO:0000256|ARBA:ARBA00004302}.
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DR EMBL; KB528689; EMP35428.1; -; Genomic_DNA.
DR AlphaFoldDB; M7BTL3; -.
DR STRING; 8469.M7BTL3; -.
DR Proteomes; UP000031443; Unassembled WGS sequence.
DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IEA:InterPro.
DR Gene3D; 2.170.240.10; Collagen IV, non-collagenous; 2.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR001442; Collagen_IV_NC.
DR InterPro; IPR036954; Collagen_IV_NC_sf.
DR InterPro; IPR016187; CTDL_fold.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF1029; COLLAGEN ALPHA-5(IV) CHAIN; 1.
DR Pfam; PF01413; C4; 2.
DR Pfam; PF01391; Collagen; 12.
DR SMART; SM00111; C4; 2.
DR SUPFAM; SSF56436; C-type lectin-like; 2.
DR PROSITE; PS51403; NC1_IV; 2.
PE 4: Predicted;
KW Basement membrane {ECO:0000256|ARBA:ARBA00022869};
KW Collagen {ECO:0000256|ARBA:ARBA00023119, ECO:0000313|EMBL:EMP35428.1};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Reference proteome {ECO:0000313|Proteomes:UP000031443};
KW Secreted {ECO:0000256|ARBA:ARBA00022530}.
FT DOMAIN 828..870
FT /note="Collagen IV NC1"
FT /evidence="ECO:0000259|PROSITE:PS51403"
FT DOMAIN 954..1037
FT /note="Collagen IV NC1"
FT /evidence="ECO:0000259|PROSITE:PS51403"
FT REGION 1..825
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 927..949
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..262
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..331
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..377
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..648
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 744..770
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EMP35428.1"
SQ SEQUENCE 1037 AA; 99008 MW; 32D731E5474B8252 CRC64;
SPGFPGSKGE KGLTGLTGLV GPPGFPGPPG APGRPGSKGD PGDSLAFPGL KGDKGDTGFP
GPPGLPGIDG SPGREGLPGL PGSKGEPGGV AFKGGMGPPG DPGVSGLPGD RGPMGPPGFG
PQGPTGEKGI QGVSGRPGPP GVPGPKGEPG ETITESGVPG SPGPPGRNGE VGLPGDPGLP
GQPGLSGIPG PKGDPGIPGI GLPGPPGLKG FPGMAGPPGA PGAPGRPGLE GPPGQSGFPG
QKGDPGFGVP GPPGPPGPPG FKGVPGLKGD PGFPGNPGFP GQSGSDGTPG PKGDPGASGP
PGLVGPPGFP GIGGQGPPGQ PGPPGPVGPP GLQGVPGEKG DPGPPGFDIP GPPGDRGSPG
FPGTPGLIGP PGSPGPPGRD GISGFPGAKG EMGVMGAPGP QGPPGTPGRN GLPGPKGSDG
LPGQPGPSGL AGQKGTKGET GLPGPPGQVD PSQLGSKGEK GEPGIPGISG VSGQKGYQGL
PGDPGPPGFN GQPGAPGLSG PKGEPGLPGQ SGPAGPPGQK GAMGETGLPG IPGIKGFQGI
AGRPGQPGPP GFPGLKGEKG NPGLSDIGIP GPKGDTGFPG YPGNPGSKGT PGNPGLAGLP
GNPGAKGEAG LPGFPGTPGI PGPKGIDGPP GNPGLPGSPG PPGDVGRPGT PGLPGEKGQP
GRDGIPGPAG QKGEPGLPGP EGPRGPPGNG GFKGEKGNPG MKGPIGPPGA IGFKGDQGPS
GPPGPPGLPG PSGQTIVVKG DSGPPGPPGQ PGLSGPPGLP GPPGLPGPIG LPGDPGRDGL
PGFDGPGGRK GERGLPGQPG FQGTQGPPGP DGLQGPPGPP GTASVAHGFL ITRHSQTTDT
PLCPQGTIRI YDGFSLLYVQ GNERAHGQDL AASQCYSIWV ANTAGQSRQK EIVLNGPIYI
SENISVNIKA NGGCGKRHRP RDVLAALPTA PIGPERRTAA SGSRDRPNLW TRQHTSAGAE
GSGQALASPG SCLEEFRSAP FIECHGRGTC NYYANSYSFW LATVEISEMF SKPQSETLKA
GDLRTRISRC QVCMKRT
//
