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Database: UniProt
Entry: W5UMU7_ICTPU
LinkDB: W5UMU7_ICTPU
Original site: W5UMU7_ICTPU 
ID   W5UMU7_ICTPU            Unreviewed;      1495 AA.
AC   W5UMU7;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Collagen alpha-1(II) chain {ECO:0000313|EMBL:AHH43065.1};
GN   Name=col2a1 {ECO:0000313|EMBL:AHH43065.1};
OS   Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC   Ictaluridae; Ictalurus.
OX   NCBI_TaxID=7998 {ECO:0000313|EMBL:AHH43065.1};
RN   [1] {ECO:0000313|EMBL:AHH43065.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Mixed {ECO:0000313|EMBL:AHH43065.1};
RX   PubMed=23127152; DOI=10.1186/1471-2164-13-595;
RA   Liu S., Zhang Y., Zhou Z., Waldbieser G., Sun F., Lu J., Zhang J.,
RA   Jiang Y., Zhang H., Wang X., Rajendran K.V., Khoo L., Kucuktas H.,
RA   Peatman E., Liu Z.;
RT   "Efficient assembly and annotation of the transcriptome of catfish by RNA-
RT   Seq analysis of a doubled haploid homozygote.";
RL   BMC Genomics 13:595-595(2012).
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DR   EMBL; JT419402; AHH43065.1; -; mRNA.
DR   GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR   GO; GO:0005201; F:extracellular matrix structural constituent; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.120.1000; -; 1.
DR   Gene3D; 6.20.200.20; -; 1.
DR   InterPro; IPR008160; Collagen.
DR   InterPro; IPR000885; Fib_collagen_C.
DR   InterPro; IPR001007; VWF_dom.
DR   NCBIfam; NF040941; GGGWT_bact; 1.
DR   PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR   PANTHER; PTHR24023:SF58; COLLAGEN ALPHA-1(II) CHAIN; 1.
DR   Pfam; PF01410; COLFI; 1.
DR   Pfam; PF01391; Collagen; 3.
DR   Pfam; PF00093; VWC; 1.
DR   SMART; SM00038; COLFI; 1.
DR   SMART; SM00214; VWC; 1.
DR   SUPFAM; SSF57603; FnI-like domain; 1.
DR   PROSITE; PS51461; NC1_FIB; 1.
DR   PROSITE; PS01208; VWFC_1; 1.
DR   PROSITE; PS50184; VWFC_2; 1.
PE   2: Evidence at transcript level;
KW   Collagen {ECO:0000313|EMBL:AHH43065.1};
KW   Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydroxylation {ECO:0000256|ARBA:ARBA00023278};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Secreted {ECO:0000256|ARBA:ARBA00022530}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..1495
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004874571"
FT   DOMAIN          34..92
FT                   /note="VWFC"
FT                   /evidence="ECO:0000259|PROSITE:PS50184"
FT   DOMAIN          1264..1495
FT                   /note="Fibrillar collagen NC1"
FT                   /evidence="ECO:0000259|PROSITE:PS51461"
FT   REGION          98..1251
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        219..233
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        795..820
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        905..929
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1122..1136
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1146..1160
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1205..1220
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1495 AA;  145231 MW;  ABB0B2BF47C990E8 CRC64;
     MMSFVHSRIF LFLALSLAQV LFVKCQDGNS GDELSCFEDG QVYTNRDVWK PEPCRICVCD
     SGTILCDDVQ CDEVINCEKV IIPDGECCPV CQSTFPDRDG GGGGDHNSRV YKGQKGEPGD
     VPIITGLPGR QGPMGPPGSP GFRGDQGPKG RPGVRGPPGY DGEPGIPGQP GEPGPPGHPP
     GGQLSSQMAE GFGGDKAAGQ HAMIPGQRGE AGARGPPGPN GLAGPPGPQG APGEPGDTGP
     MGPAGQRGPE GPPGKPGEDG EAGTSGSTGE TGFPGSAGAR GFPGTPGPPG LKGHRGHQGP
     EGLKGERGAV GSKGESGGTG PMGVPGPMGP RGMPGERGRP GPSGAPGTRG AQGNVGKPGP
     MGPLGLSGSA GYPGAPGMKG QPGPTGVRGP EGPQGPRGES GPQGRPGPIG LQGPMGTDGG
     PGTKGPVGTV GPQGPIGLPG PHGPPGPQGS TGQPGIKGQL GDVGVPGFKG EAGPKGEQGP
     PGAQGSIGPQ GEEGKRGLRG DPGSVGPPGP VGERGAPGNR GFPGQDGLQG AKGAVGERGI
     SGVSGPKGST GDPGRTGEPG LPGARGLTGT PGVQGAEGKP GPLGPTGEDG RPGPPGSIGT
     KGPEGSMGLP GPRGFSGDPG KPGEQGSPGP PGQRGLPGKE GEVGPLGPTG PPGPAGDRGE
     QGPPGMHGFQ GLPGPAGPVG EGGKPGDQGI HGEGGPVGPL GPRGERGTPG ERGELGSPGL
     QGPKGIPGAP GSDGPKGSPG PAGTVGDLGP PGLQGMPGER GISGPPGPKG DRGSVGEKGS
     EGTSGNDGAR GLPGPLGPAG PPGPSGEKGE PGPKGPPGPH GSRAMPGSRG EPGPTGAVGF
     PGPPGPDGQP GVKGEPGEPG QKGDAGSPGH QGLSGPPGPM GPVGVAGPKG GRGTQGAPGP
     TGFPGSPGKV GPPGPTGSLG QPGPVGPPGK EGPSGLRGDH GPPGRQGERG QAGPAGSPGD
     KGDPGEDGPT GPDGPPGPAG TTGQRGIVGL PGQRGERGML GLPGPAGPPG KAGTSGSPGD
     KGPPGPVGAP GANGPRGDAG PDGPAGADGP PGKEGVIGER GDRGDSGPEG LTGPRGAPGT
     PGPVGTTGGP GKRGDVGSRG PVGPPGPAGK RGLPGPQGPR GDKGELGDHG ERGQKGHRGY
     TGLQGLPGSP GTTGDQGPSG IVGPSGQRGP PGPIGPPGKE GYIGQPGPMG PPGSRGISGD
     IGPEGPPGEP GPPGLPGSPG PPIAAMEDMF GGPQDYDAGP PPPEFPEDEA LPKSNLTDMF
     QADPGVQATL KALSSQIESM RSPDGSKKHP ARTCEDLKQC YPLKKSGEYW VDPNQGSSED
     AIKVYCNMET GETCISAEPS SIPRKSWWST PGNKPVWFGA MNGGTYFTYG NKDQPANSVT
     VQMTFIRLLS KEASQTITYH CKNAVGYKDE ATGNLKKAVI LKASNDLELK AEGNNRFRYT
     VLEDSCSQAN SNWGKTVFEY RTQKTARLPI VDIATVDVGR PDQEFGIDIG PVCFL
//
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