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Database: UniProt
Entry: H9ERC9_MACMU
LinkDB: H9ERC9_MACMU
Original site: H9ERC9_MACMU 
ID   H9ERC9_MACMU            Unreviewed;      1685 AA.
AC   H9ERC9;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2012, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   SubName: Full=Collagen alpha-5(IV) chain isoform 1 {ECO:0000313|EMBL:AFE64938.1};
GN   Name=COL4A5 {ECO:0000313|EMBL:AFE64938.1};
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544 {ECO:0000313|EMBL:AFE64938.1};
RN   [1] {ECO:0000313|EMBL:AFE64938.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Caudate {ECO:0000313|EMBL:AFE64938.1};
RX   PubMed=25319552; DOI=10.1186/1745-6150-9-20;
RA   Zimin A.V., Cornish A.S., Maudhoo M.D., Gibbs R.M., Zhang X., Pandey S.,
RA   Meehan D.T., Wipfler K., Bosinger S.E., Johnson Z.P., Tharp G.K.,
RA   Marcais G., Roberts M., Ferguson B., Fox H.S., Treangen T., Salzberg S.L.,
RA   Yorke J.A., Norgren R.B.Jr.;
RT   "A new rhesus macaque assembly and annotation for next-generation
RT   sequencing analyses.";
RL   Biol. Direct 9:20-20(2014).
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; JU321182; AFE64938.1; -; mRNA.
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:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
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; 20.
DR   SMART; SM00111; C4; 2.
DR   SUPFAM; SSF56436; C-type lectin-like; 2.
DR   PROSITE; PS51403; NC1_IV; 1.
PE   2: Evidence at transcript level;
KW   Basement membrane {ECO:0000256|ARBA:ARBA00022869};
KW   Collagen {ECO:0000256|ARBA:ARBA00023119, ECO:0000313|EMBL:AFE64938.1};
KW   Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW   Hydroxylation {ECO:0000256|ARBA:ARBA00023278};
KW   Lectin {ECO:0000256|ARBA:ARBA00022734};
KW   Secreted {ECO:0000256|ARBA:ARBA00022530}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..1685
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003619957"
FT   DOMAIN          1461..1685
FT                   /note="Collagen IV NC1"
FT                   /evidence="ECO:0000259|PROSITE:PS51403"
FT   REGION          49..1460
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        87..105
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        139..153
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        171..213
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        265..279
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        286..303
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        380..402
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        415..462
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        607..629
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        705..728
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        740..766
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        806..833
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        849..878
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        997..1018
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1039..1054
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1122..1145
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1232..1273
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1394..1408
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1685 AA;  161081 MW;  41B135C0761BEA7D CRC64;
     MKLRGVSQAA GLFLLALSLW GQPAEAAACY GCSPGSKCDC SGIKGEKGER GFPGLEGHPG
     LPGFPGPEGP PGPRGQKGDD GIPGPPGPKG IRGPPGLPGF PGTPGLPGMP GHDGAPGPQG
     IPGCNGTKGE RGFPGSPGFP GLQGPPGPPG IPGMKGEPGS IIMSSLPGPK GNPGYPGPPG
     IQGLPGPTGI PGPIGPPGPP GLMGPPGPPG LPGPKGNMGL NFQGPKGEKG EQGLQGPPGP
     PGQISEQKRP IDVEFQKGDQ GLPGDRGPPG PPGIRGPPGP PGGEKGEKGE QGEPGKRGKP
     GKDGENGQPG IPGLPGDPGY PGEPGRDGEK GQKGDIGPPG PPGLVIPRPG TGITIGEKGN
     IGLPGLPGEK GERGFPGIQG PPGLPGPPGA AVVGPPGPPG FPGERGQKGD EGPPGISIPG
     PPGLDGQPGA PGLPGPPGPP GPHIPPSDEI CEAGPPGPPG SPGDKGLQGE QGMKGDKGDT
     CFNCIGTGIS GPPGQPGLPG LPGPPGSLGF PGQKGEKGQA GATGSKGLPG IPGAPGAPGF
     PGSKGEPGDI LTFPGMKGDK GELGSPGAPG LPGLPGTPGQ DGLPGLPGPK GEPGGITFKG
     ERGPPGNPGL PGLPGNIGPM GPPGFGPPGP VGEKGIQGVA GNPGQPGIPG PKGDPGQTIT
     QPGKPGLPGN PGRDGEVGLP GDPGLPGQPG LPGIPGSKGE PGIPGIGLPG PPGPKGFPGI
     PGPPGAPGTP GRIGLEGLPG PPGFPGPKGE PGFALPGPPG PPGLPGFKGT LGPKGDRGFP
     GPPGPPGRTG IDGLPGPKGD VGPNGQPGPM GPPGLPGIGV QGPPGPPGIP GPIGQPGLHG
     IPGEKGDPGP PGLDVPGPPG ERGSPGIPGA PGSIGPPGSP GLPGKAGASG FPGTKGEMGM
     MGPPGPPGPL GIPGRSGVPG LKGDDGLQGQ PGLPGPAGEK GSKGEPGLPG PPGPMDPNLL
     GSKGEKGEPG LPGIPGVSGP KGYQGLPGDP GQPGLSGQPG LPGPPGPKGN PGLPGQPGLI
     GPPGLKGTIG DMGFPGPQGV EGPPGPPGAP GQPGSPGLPG QKGDKGDPGI SSIGLPGLPG
     PKGEPGLPGY PGNPGIKGSV GDPGLPGLPG TPGAKGQPGL PGFPGTPGPP GPKGISGPPG
     NPGLPGETGP VGGGGRPGQP GPPGEKGKPG QDGIPGPAGQ KGEPGQPGFG NPGPPGLPGL
     SGQKGDGGLP GIPGNPGLPG PKGEPGFHGF PGVQGPPGPP GSPGPALEGP KGNPGPQGPP
     GRPGLPGPEG PPGLPGNGGI KGEKGNPGQP GLPGLPGLKG DQGPPGLQGN PGRPGLNGMK
     GDPGLPGVPG FSGMKGPSGI PGSAGPEGEP GLTGPPGPPG LPGPSGQSII IKGDAGPPGI
     PGQPGLKGLP GPQGPQGLPG PTGPPGDPGR NGLPGFDGAG GRKGDPGLPG QPGTRGLDGP
     PGPDGLQGPP GPPGTSSTAH GFLITRHSQT TDAPQCPQGT LQIYEGFSLL YVQGNKRAHG
     QDLGTAGSCL RRFSTMPFMF CNINNVCNFA SRNDYSYWLS TPEPMPVSMQ PLKGQSIQPF
     ISRCAVCEAP AVVIAVHSQT IQIPRCPQGW DSLWIGYSFM MHTSAGAEGS GQALASPGSC
     LEEFRSAPFI ECHGRGTCNY YANSYSFWLA TVDVSDMFSK PQSETLKAGD LRTRISRCQV
     CMKRT
//
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