ID A0A384BAB4_BALAS Unreviewed; 1685 AA.
AC A0A384BAB4;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Collagen alpha-5(IV) chain isoform X2 {ECO:0000313|RefSeq:XP_007196448.1};
GN Name=COL4A5 {ECO:0000313|RefSeq:XP_007196448.1};
OS Balaenoptera acutorostrata scammoni (North Pacific minke whale)
OS (Balaenoptera davidsoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti;
OC Balaenopteridae; Balaenoptera.
OX NCBI_TaxID=310752 {ECO:0000313|Proteomes:UP000261681, ECO:0000313|RefSeq:XP_007196448.1};
RN [1] {ECO:0000313|RefSeq:XP_007196448.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_007196448.1};
RG RefSeq;
RL Submitted (JAN-2023) to UniProtKB.
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 RefSeq; XP_007196448.1; XM_007196386.1.
DR GeneID; 103009501; -.
DR CTD; 1287; -.
DR OrthoDB; 2882192at2759; -.
DR Proteomes; UP000261681; Unplaced.
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:SF1029; COLLAGEN ALPHA-5(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 4: Predicted;
KW Basement membrane {ECO:0000256|ARBA:ARBA00022869};
KW Collagen {ECO:0000256|ARBA:ARBA00023119,
KW ECO:0000313|RefSeq:XP_007196448.1};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Reference proteome {ECO:0000313|Proteomes:UP000261681};
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_5016863532"
FT DOMAIN 1461..1685
FT /note="Collagen IV NC1"
FT /evidence="ECO:0000259|PROSITE:PS51403"
FT REGION 49..749
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 770..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 289..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 429..462
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 817..833
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 849..880
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1040..1054
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1123..1166
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1232..1270
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; 161212 MW; D9AAB8C2EE6D3D58 CRC64;
MKLRGVSLAA GLFLLALSLW GQPAEAAACY GCSPGSKCDC SGIKGEKGER GFPGLEGHPG
LPGFPGPEGP PGPRGQKGSD GIPGPPGPKG KRGPPGLPGF PGTPGLPGMP GHDGAPGPQG
IPGCNGTKGE RGFPGSPGFP GLQGPPGPPG IPGMKGEPGS VIVSSLPGPK GNPGFPGPPG
IQGPAGPTGI PGPIGPLGPP GLMGPPGPPG LPGPKGNMGL NFQGPKGEKG EQGLQGPPGP
PGQISEQKRP IDVEFQKGDQ GLPGDRGPPG PPGIRGPPGP PGGMKGEKGE QGEPGKRGKP
GKDGENGQPG IPGLPGDPGY PGEPGRDGEK GQKGDIGPTG PPGLVIPRPG TGVTVGEKGN
IGLPGLPGEK GERGFPGIQG PPGLPGPPGL AVTGPPGPPG FPGERGQKGD EGPPGISIPG
SPGLDGQPGA PGLPGPPGPP GPHIPPSDEV CEAGPPGPPG SPGDRGLQGE QGVKGDKGDT
CFNCIGTGVS GPPGEPGLPG LPGPPGSLGF PGQKGEKGHA GATGPKGLTG IPGAPGAPGF
PGPKGEPGDI LTLPRMKGDK GDLGSPGAPG LPGLPGTPGQ DGLPGLPGPK GEPGGIAFKG
ERGPPGNPGL PGLPGNRGPM GPLGFGPPGP PGEKGIQGVA GNPGQPGIPG PKGDPGQTIT
QPGKPGLPGK PGKDGEVGLP GEPGLPGQPG LPGIPGSKGE PGIPGIGLPG PPGPKGFPGI
PGPPGAPGTP GRIGLEGPSG PPGFPGLKGE PGFGLPGPPG PPGLPGFKGI LGPKGDRGFP
GPQGPPGQAG LDGLPGPKGD IGPNGQPGAM GPPGLPGTGV QGPPGPPGIP GPIGQPGLHG
IPGEKGDPGP PGFDVPGPPG ERGSPGIPGA PGPMGPPGSP GFPGKAGASG FPGAKGEMGM
MGPPGPTGPL GIPGRSGVPG LKGDDGLQGQ PGLPGPAGEK GSKGEPGLPG LPGPMDPDLL
GSKGEKGDPG LPGIPGVAGP KGYQGSPGDP GQPGLSGQPG LPGPSGPKGN PGLPGKPGLT
GPPGLKGNIG DMGFPGPQGA KGSPGPPGVP GQPGSPGLPG QKGEKGDPGI SGIGLPGLPG
PKGEPGLPGY PGNPGIKGAM GDTGLPGLPG TPGAKGQPGL PGFPGTPGLP GPKGINGPPG
NPGLPGEPGP VGGGGRPGPP GPPGEKGKPG QDGIPGPAGQ KGEPGQPGFG IPGPPGLPGL
SGQKGDGGLP GIPGNPGLPG PKGEPGFHGF PGLQGPPGPP GSPGPALEGP KGNPGPQGPP
GRPGLPGPEG PRGLPGIGGI KGERGNPGQP GQPGLSGLKG DQGPPGLQGN PGRPGLNGMK
GDPGLPGVPG FPGMKGPSGE PGSTGPEGDP GLIGPPGPPG LPGPSGQSIV IKGDAGPPGV
PGQPGLKGLP GLPGPQGLPG PIGPPGDPGR NGLPGFDGAG GHKGDPGLPG QPGIRGLDGP
PGPDGLQGPP GPPGTSPVAH GFLITRHSQT TDAPQCPQGT IQFYEGFSLL YVQGNKRAHG
QDLGTAGSCL RRFSTMPFMF CNINNVCNFA SRNDYSYWLS TPEPMPMSME PLKGQSIQPF
ISRCAVCEAP AVVIAVHSQT IQIPRCPQGW DSLWIGYSFM MHTSAGAEGS GQALASPGSC
LEEFRSAPFI ECHGRGTCNY YANSYSFWLA TVDVSDMFSK PQSETLKAGD LRTRISRCQV
CMKRT
//