ID M7CHE6_CHEMY Unreviewed; 1568 AA.
AC M7CHE6;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Collagen alpha-6(IV) chain {ECO:0000313|EMBL:EMP40317.1};
DE Flags: Fragment;
GN ORFNames=UY3_02480 {ECO:0000313|EMBL:EMP40317.1};
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:EMP40317.1, 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; KB514175; EMP40317.1; -; Genomic_DNA.
DR STRING; 8469.M7CHE6; -.
DR eggNOG; KOG3544; Eukaryota.
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; 1.
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:SF588; COLLAGEN ALPHA-2(IV) CHAIN; 1.
DR Pfam; PF01413; C4; 2.
DR Pfam; PF01391; Collagen; 16.
DR SMART; SM00111; C4; 2.
DR SUPFAM; SSF56436; C-type lectin-like; 2.
DR PROSITE; PS51403; NC1_IV; 1.
PE 4: Predicted;
KW Basement membrane {ECO:0000256|ARBA:ARBA00022869};
KW Collagen {ECO:0000256|ARBA:ARBA00023119, ECO:0000313|EMBL:EMP40317.1};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Reference proteome {ECO:0000313|Proteomes:UP000031443};
KW Secreted {ECO:0000256|ARBA:ARBA00022530}.
FT DOMAIN 1344..1568
FT /note="Collagen IV NC1"
FT /evidence="ECO:0000259|PROSITE:PS51403"
FT REGION 1..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 210..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 455..843
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 858..1340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 759..773
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EMP40317.1"
FT NON_TER 1568
FT /evidence="ECO:0000313|EMBL:EMP40317.1"
SQ SEQUENCE 1568 AA; 153581 MW; 4193D9D59C85671E CRC64;
GYPGVEGSRG KPALDGCNGS RGDPGFPGET GCIGPRGSFG VLGQKGEKGN SAYISDFIRG
DPGARGEPGS PGTPGARGLR GPHGLPGQPG LQGAPGLPGL QGEQGNPGTG VDGQKGEPGD
VGPPGSPGQP LLVGPPDSFL VKGEKGVKGM PGLVGPKGSH GPKGAPGNGE KGEKGIPGDP
GMQGSPGSCG SLGFPGIKGA SGVPGVPGQA GYAGLKGDRG ERGQPGLPGV FGTPPVAMKG
SRGDPGLPGP SGDDGLIGLT GPPGPSGRPG EDGTRACGQQ GPKGSHGDPG LPGTAESTPG
RPGSPGAPGL PGAPGRQGLP GPPGKINNIS VLFCHGRGPR GHQGIKGQMG PMGRRGEKGE
KGNSKLFSYI CIGNHGHCSC DLGSAGPPGR RGPPGRQGRK GQTGFPASYG EKGDPGFSGT
IGSTGLPGKP GSSGIAGEKG EKGDLAIVKI KGIKGKRGPL GVPGLPGQKG TAGRDGDPGL
PGERGIQGDG GSALPGDKGF LGAPGLPGSR GPMGPSGLGF PGPQGIRGHP GDPGSTGISG
PPGPKGQRGD IHCYVPPYPG SPGPPGFQGA QGPKGLRGPP GPPGPNGFDG QKGQRGKPGT
SGDIGPDGFR GNAGDPGDEG ERGSSPDGAP GFPGSPGLSG QKGVPGDTSY GLPGIPGHRG
LPGLPGLQGI RGESGTPGPQ GQSGRPGFPG ATGLRGRKGE IGAPGSPGQP CDKGLQGPPG
QLGVLGQRGP PGLPGFKGQK GDMGPPGPAG MKGLPGSPGV PGSPGPPGPR GYPGLPGSNG
LLGLPGQRGS KGIQGIQGFP GISGKGGQTG IPGGHGEQGE MGSRGPSGEC GDGGQKGERG
AQGDSGFITL WLEKGQKGEQ GLPGEAGFPG ETGEKGSLGI RGIPGFPGKV GLPGTQKGEP
GDRGQIGFPG LPGSPGLGGL RGITGFQGQR GDQGERGLPG IPGCPGRDGA KGLKGNRGDS
GSQYGPPGQR GPPGDHGSPG PCGFPGERGL PGFQGEPGRQ GPKGMPGSPG AKGFPGAICD
LGLPGVPGGQ GNTGPLGAAG LPGSPGPPGR KGLSGLPGLD GLNGLQGQKG SPGDPGKSEI
GPPGYTGAPG PKGDKGEPGQ PGISLPGPPG DTGLPGHPGR TGDTGPAGSV GRSPETAASG
PPGDQGPPGS HGIRGLPGNP GPPGKTIFVK GDPGEFGVPG APGIPGQPGQ QGAKGFPGNR
GRRGLKGPMG NPGLQGPPGP VGPSGDRGFQ GQPGPRGPEG DPGEPGKTEH SPCPKTPGPR
GVIGQRGAEG SVGFPGPIGY PGPPGSKGEE GLFGLPGQDG SPGPPGPSGD QGVIGEQGYT
GPEGPPGQAG IPGPPAPETR AASGFLLILH SQSDKEPFCP EGMPRLWTGY SLLYLEGQEK
AHNQDLGLAG SCLPVFNTMP FVFCNIHQVC YYASRNDKSY WLSTAAPLPM MPLSEDEIQP
YISRCAVCEA SAQAVAVHSQ DQSIPPCPLN WRSLWIGYSF LMHTGSGDQG GGQSLMSTGS
CLEDFRSAPF IECQGQRGTC QFFANEYSFW LTIVRPELQF VSASLSETLK EGHEQRKKIS
RCQVCMKH
//
