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Database: UniProt
Entry: H2TMY0_TAKRU
LinkDB: H2TMY0_TAKRU
Original site: H2TMY0_TAKRU 
ID   H2TMY0_TAKRU            Unreviewed;      1321 AA.
AC   H2TMY0;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 3.
DT   27-MAR-2024, entry version 55.
DE   RecName: Full=Collagen type II alpha 1 chain {ECO:0008006|Google:ProtNLM};
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000026036.3, ECO:0000313|Proteomes:UP000005226};
RN   [1] {ECO:0000313|Ensembl:ENSTRUP00000026036.3, ECO:0000313|Proteomes:UP000005226}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21551351;
RA   Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA   Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT   "Integration of the genetic map and genome assembly of fugu facilitates
RT   insights into distinct features of genome evolution in teleosts and
RT   mammals.";
RL   Genome Biol. Evol. 3:424-442(2011).
RN   [2] {ECO:0000313|Ensembl:ENSTRUP00000026036.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   STRING; 31033.ENSTRUP00000078264; -.
DR   Ensembl; ENSTRUT00000026141.3; ENSTRUP00000026036.3; ENSTRUG00000010345.3.
DR   GeneTree; ENSGT00940000155639; -.
DR   Proteomes; UP000005226; Chromosome 19.
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; 1.20.5.320; 6-Phosphogluconate Dehydrogenase, domain 3; 1.
DR   Gene3D; 2.10.70.10; Complement Module, domain 1; 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; 10.
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   4: Predicted;
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   Reference proteome {ECO:0000313|Proteomes:UP000005226};
KW   Secreted {ECO:0000256|ARBA:ARBA00022530}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..1321
FT                   /note="Collagen type II alpha 1 chain"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5025499803"
FT   DOMAIN          35..93
FT                   /note="VWFC"
FT                   /evidence="ECO:0000259|PROSITE:PS50184"
FT   DOMAIN          1087..1321
FT                   /note="Fibrillar collagen NC1"
FT                   /evidence="ECO:0000259|PROSITE:PS51461"
FT   REGION          129..496
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          515..545
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          557..679
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          694..1071
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        288..302
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        939..957
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1035..1049
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1321 AA;  129772 MW;  1859A9803BC185FA CRC64;
     MFSFMDSRIV LLLVASQVCL LTVVRCQEED DQATLSCMQD GQRYSDKDVW KPEPCRICVC
     DTGTVLCDEI VCEELKDCRN PEIPFGECCP ICAADQSPPI GRNLFISHFI INKLLHILML
     FVLEEGMKGS AGPRGRDGEP GTPGNPGSPG PPGPPGLGGN FAAQMAGGFD EKAGGGAQMG
     VMQGPMVSKR SGPMGPRGPP GPSGKAGEDG ARGFPGTPGL PGIKGHRGYS GIDGAKGETG
     AVGSKGESGA PGENGAPGPM GPRGLPGERG RPGPSGVAGA RGNDGLPGPA GPPGPVGPSG
     APGFPGSPGS KGEAGPTGAR GPEGAQGPRG ESGTPGSPGP SGASGNPGTD GIPGAKGSAG
     AHGIAGAPGF PGPRGPPGPQ GATGPLGPKG TSGDPGIAGF KGEAGPKGEI GPAGLQGAPG
     QQGEEGKRGP RGEPGAAGPI GPPGERGAPG NRGFPGQDGL AGSKGAPGER GTSGASGPKG
     ANGDPGRPGE SGLPGARVRA DHCHNCYMCG APGEDGRPGP PGPQGARGQP GVMGFPGPKG
     ASVSTDTFGQ IQKSLLRLGG VPGEAGASGT TGPRGERGFP GERGAAGPQG LQGPRGLPGT
     PGTDGPKGAI GPHGSLGAQG PPGLQGMPGE RGGAGIPGPK GDRGDLGEKG PEGAPGKDGA
     RGLTGPIGPP GPSGPNGEKV SDIYLLQALL LQGSDGQPGI KGEQGETGQK GDAGAPGPQG
     PSGAPGPAGP TGVSGPKGAR GAQGPPGATG FPGAAGRVGP PGPNGNPGPA GPAGSPGKDG
     PKGIRGDGGP PGRQGDAGLR GPAGPSGEKG DAGEDGPVGP PGPSGPQGLG GQRGIVGLPG
     QRGERGFPGL PGPSGEPGKQ GAPGTGGDRG PPGPVGPPGL TGPAGESGRE GNPGSDGPPG
     RDGATGIKGD RGDTGPTGSP GAPGAPGAQG PVGQTGKQGD RGESVSSNSN KHGNTRFICF
     TGPQGPRGDK GEGGESGERG QKGHRGFTGL QGLPGPPGPP GPVGPSGKDG AFGLPGPIGP
     PGPRGRSGET GPAGPPGNSG PPGLPGPPGP GIDMSAFAGL GQTEKGPDPL RYMRADQASG
     NLRQHDAEVD ATLKSLNNQI ENIRSPEGSK KNPARTCRDL KLCHPDWKSG EYWIDPNQGC
     TVDAIKVYCD METGETCVQP KPSSISRKNW WTSKSKDRKH VWFSETMNGG FHFSYGDDSL
     APNTAAIQMT FLRLLSTEAS QNLTYHCKNS VAYMDASTGN LKKAVLLQGS NDVEIRAEGN
     SRFTYSVLED GCTKHTGQWG KTLIEYRSQK TSRLPIVDIA PMDIGEAHQE FGVEVGAVCF
     L
//
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