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Database: UniProt
Entry: A0A3Q2DZX0_CYPVA
LinkDB: A0A3Q2DZX0_CYPVA
Original site: A0A3Q2DZX0_CYPVA 
ID   A0A3Q2DZX0_CYPVA        Unreviewed;      1145 AA.
AC   A0A3Q2DZX0;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Collagen type II alpha 1 chain {ECO:0000313|Ensembl:ENSCVAP00000025382.1};
GN   Name=COL2A1 {ECO:0000313|Ensembl:ENSCVAP00000025382.1};
OS   Cyprinodon variegatus (Sheepshead minnow).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Cyprinodontidae;
OC   Cyprinodon.
OX   NCBI_TaxID=28743 {ECO:0000313|Ensembl:ENSCVAP00000025382.1, ECO:0000313|Proteomes:UP000265020};
RN   [1] {ECO:0000313|Ensembl:ENSCVAP00000025382.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   AlphaFoldDB; A0A3Q2DZX0; -.
DR   Ensembl; ENSCVAT00000001779.1; ENSCVAP00000025382.1; ENSCVAG00000015242.1.
DR   GeneTree; ENSGT00940000155224; -.
DR   Proteomes; UP000265020; Unplaced.
DR   GO; GO:0016020; C:membrane; 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; 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   PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR   PANTHER; PTHR24023:SF58; COLLAGEN ALPHA-1(II) CHAIN; 1.
DR   Pfam; PF01410; COLFI; 1.
DR   Pfam; PF01391; Collagen; 2.
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   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265020};
KW   Secreted {ECO:0000256|ARBA:ARBA00022530}; Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..1145
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018575116"
FT   TRANSMEM        99..118
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        158..177
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          36..94
FT                   /note="VWFC"
FT                   /evidence="ECO:0000259|PROSITE:PS50184"
FT   DOMAIN          911..1145
FT                   /note="Fibrillar collagen NC1"
FT                   /evidence="ECO:0000259|PROSITE:PS51461"
FT   REGION          215..444
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          467..892
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        283..299
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        314..328
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        639..653
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        858..875
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1145 AA;  113709 MW;  394455C67A1712EC CRC64;
     MLSFMDSRTL LLLVASHVFL LAVVRCQRED NQEEDFICSQ DGQSYNDKDI WKPEPCRICV
     CDKGMVLCDD IVCEELKDCP KPEIPFGECC PICAADQPSS FGLVLLSYLM MTGFIFPLQN
     FAAQMAGGFD EKAGGGAQMG VMQGPMVRKR PCKMKSMGFI FFHCNIVISS TILHLTAQGA
     RGFPGTPGLP GIKGHRGYPG LDGAKGETGA VGAKVGIGPR GLPGERGRPG STGAAGARGN
     DGLPGPAGPP VGIILDIGEA GPTGARGPEG AQGPRGESGT PGSPGPSGAS VSNGIITNLN
     RKKVGAPGIA GAPGFPGPRG PPGPQGATGP LGPKGTSGPV GPQGAPGPQG EEGKRGPRGE
     PGAAGPLGPP GERVSNKGLR KQGAPGERGP PGTSGAKGAT GDPGRPGEPG LPGARGAPGE
     DGRPGPPGPQ GARGQPGVMG FPGPKGATVS IFKCWCVPFQ GERGFPGERG AAGAQGLQGP
     RGLPGTPGTD GPKGAIGPAG GPGAQGPPGL QGMPGERGAA GIPGPKGDRG DVGEKGPEGA
     SGKDGARGLT GPIGPPGPAG PNGEKGESGP AGPSGPAGVR GAPVSGADGQ PGIKGEQGEA
     GQKGDAGAPG PQGPSGAPGP AVRGATGFPG AAGRVGPPGP NGNPGPPGPA GSPGKDGPKG
     VRGDGGPPGR QGDPGLRGPA GAPGEKGDAG EDGPPGPLGP SGPQGLAGQR GIVGLPGQRG
     ERGFPGLPGP SGDRGNTGPA GAPGAPGAPG APGPVGPTGK QGNRGESGPQ GPRGDKGEGG
     EAGERGQKGH RGFTGLQGLP GPPGQPGDQG ATGPAGPSGQ RGPPGPVGPA GKDGSNGLPG
     PIGPPGPRGR TGDSGPAGPP GNPGPPGPPG PPGPGIDMSA FAGLGQTEKS PDPLRYMRAD
     QAAGNLRQHD AEVDATLKSL NNQIENIRSP EGSKKNPART CRDLKLCHPD WKSGEYWIDP
     NQGCTVDAIK VFCNMETGES CVNPRPAKIP RKNWWSSKSK DSKHVWFGET MNGGFHFSYG
     DDSLAPNTAA IQMTFLRLLS TEASQNITYH CKNSVAYLDA SNSNLKKAVL LQGSNDVEIR
     AEGNSRFTYS VMEDSCTRHT GQWGKTVIEY RSQKTSRLPI VDIAPMDIGG ADQEFGVDIG
     AVCFL
//
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