ID F6R6T3_ORNAN Unreviewed; 2911 AA.
AC F6R6T3;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 2.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=Collagen type VI alpha 3 chain {ECO:0000313|Ensembl:ENSOANP00000018890.2};
GN Name=COL6A3 {ECO:0000313|Ensembl:ENSOANP00000018890.2};
OS Ornithorhynchus anatinus (Duckbill platypus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Monotremata; Ornithorhynchidae; Ornithorhynchus.
OX NCBI_TaxID=9258 {ECO:0000313|Ensembl:ENSOANP00000018890.2, ECO:0000313|Proteomes:UP000002279};
RN [1] {ECO:0000313|Ensembl:ENSOANP00000018890.2, ECO:0000313|Proteomes:UP000002279}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Glennie {ECO:0000313|Ensembl:ENSOANP00000018890.2,
RC ECO:0000313|Proteomes:UP000002279};
RX PubMed=18464734; DOI=10.1038/nature06936;
RA Warren W.C., Hillier L.W., Marshall Graves J.A., Birney E., Ponting C.P.,
RA Grutzner F., Belov K., Miller W., Clarke L., Chinwalla A.T., Yang S.P.,
RA Heger A., Locke D.P., Miethke P., Waters P.D., Veyrunes F., Fulton L.,
RA Fulton B., Graves T., Wallis J., Puente X.S., Lopez-Otin C., Ordonez G.R.,
RA Eichler E.E., Chen L., Cheng Z., Deakin J.E., Alsop A., Thompson K.,
RA Kirby P., Papenfuss A.T., Wakefield M.J., Olender T., Lancet D.,
RA Huttley G.A., Smit A.F., Pask A., Temple-Smith P., Batzer M.A.,
RA Walker J.A., Konkel M.K., Harris R.S., Whittington C.M., Wong E.S.,
RA Gemmell N.J., Buschiazzo E., Vargas Jentzsch I.M., Merkel A., Schmitz J.,
RA Zemann A., Churakov G., Kriegs J.O., Brosius J., Murchison E.P.,
RA Sachidanandam R., Smith C., Hannon G.J., Tsend-Ayush E., McMillan D.,
RA Attenborough R., Rens W., Ferguson-Smith M., Lefevre C.M., Sharp J.A.,
RA Nicholas K.R., Ray D.A., Kube M., Reinhardt R., Pringle T.H., Taylor J.,
RA Jones R.C., Nixon B., Dacheux J.L., Niwa H., Sekita Y., Huang X., Stark A.,
RA Kheradpour P., Kellis M., Flicek P., Chen Y., Webber C., Hardison R.,
RA Nelson J., Hallsworth-Pepin K., Delehaunty K., Markovic C., Minx P.,
RA Feng Y., Kremitzki C., Mitreva M., Glasscock J., Wylie T., Wohldmann P.,
RA Thiru P., Nhan M.N., Pohl C.S., Smith S.M., Hou S., Nefedov M.,
RA de Jong P.J., Renfree M.B., Mardis E.R., Wilson R.K.;
RT "Genome analysis of the platypus reveals unique signatures of evolution.";
RL Nature 453:175-183(2008).
RN [2] {ECO:0000313|Ensembl:ENSOANP00000018890.2}
RP IDENTIFICATION.
RC STRAIN=Glennie {ECO:0000313|Ensembl:ENSOANP00000018890.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR STRING; 9258.ENSOANP00000018890; -.
DR Ensembl; ENSOANT00000018893.3; ENSOANP00000018890.2; ENSOANG00000011917.3.
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00940000156462; -.
DR HOGENOM; CLU_000182_1_0_1; -.
DR InParanoid; F6R6T3; -.
DR OMA; KGGRQAN; -.
DR TreeFam; TF337483; -.
DR Proteomes; UP000002279; Chromosome 7.
DR Bgee; ENSOANG00000011917; Expressed in fibroblast and 8 other cell types or tissues.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0042383; C:sarcolemma; IEA:Ensembl.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0043491; P:phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:Ensembl.
DR GO; GO:0009411; P:response to UV; IEA:Ensembl.
DR CDD; cd00063; FN3; 1.
DR CDD; cd22629; Kunitz_collagen_alpha3_VI; 1.
DR CDD; cd01450; vWFA_subfamily_ECM; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 4.10.410.10; Pancreatic trypsin inhibitor Kunitz domain; 1.
DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 11.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR002223; Kunitz_BPTI.
DR InterPro; IPR036880; Kunitz_BPTI_sf.
DR InterPro; IPR020901; Prtase_inh_Kunz-CS.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR24020:SF82; CCHC-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24020; COLLAGEN ALPHA; 1.
DR Pfam; PF01391; Collagen; 1.
DR Pfam; PF00014; Kunitz_BPTI; 1.
DR Pfam; PF00092; VWA; 11.
DR PRINTS; PR00453; VWFADOMAIN.
DR SMART; SM00131; KU; 1.
DR SMART; SM00327; VWA; 12.
DR SUPFAM; SSF57362; BPTI-like; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF53300; vWA-like; 12.
DR PROSITE; PS00280; BPTI_KUNITZ_1; 1.
DR PROSITE; PS50279; BPTI_KUNITZ_2; 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS50234; VWFA; 11.
PE 4: Predicted;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Reference proteome {ECO:0000313|Proteomes:UP000002279};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 26..200
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT DOMAIN 229..402
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT DOMAIN 432..608
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT DOMAIN 626..803
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT DOMAIN 824..996
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT DOMAIN 1015..1191
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT DOMAIN 1218..1389
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT DOMAIN 1421..1598
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT DOMAIN 1622..1799
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT DOMAIN 2153..2336
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT DOMAIN 2369..2565
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT DOMAIN 2730..2822
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 2850..2901
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT REGION 1598..1617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2089..2110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2613..2649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2678..2717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2812..2831
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2911 AA; 319226 MW; 95156059D97766BE CRC64;
MIFDELKKSL KLMCFFKDVK IGVAADIIFL VDSSWSIGKE HFQLVREFLY DVIKSLDVGD
NDYRFALVQF SGNPHTEFLL NTYHANQDVL AHVATMPYLG GGSKTGKGLD YLIHHHLTKA
SGSRASDGIP QVIIVLTDGQ SQDDIVLPTA ELKSADVTVF AIGVQDAEEG ELKEIASEPL
DMHVFNIETF TALHDLVGDL VSCVQTSMTP EMAGAKEILK DITAQESADL IFLIDGSNNI
GSVHFSAIRD FLVNFLERLA IGPQQIQVGV VQYSDEPSTV FSLNSYSTKA DVLDAVKALR
FAGGEGANIG AALEFVVENH FTQATGSRVE EGVPQVLVLI SAGQSSDEVD DGVVALKQAS
IFSFGLGAQD ADKAELQHIA TDESFVFTTP EFRSLGDLQE QLLPYIVGVA QRNIVLQPPT
IITQVVEVNK RDIVFLIDGS SSLGVASFYA IREFLVRVIQ KLEIGQDLIQ VAVAQYADSV
KPEFYFNTFQ TKRDIVMALR RVKFLDGPAR NTGSALDYVR NYFFTSSAGH RAAEGVPKLL
VLLTGGKSLD DVHQPAQELK RNGILAFAIG SRLAAKDELE DIAFDSSLVF SPDEFKNVPL
QGILLNFLAP LRTLSGTMQV HVNKRDIIFL LDGSLNVGNA NFHYVRDFVM NLVNSLDVGR
DNIRVGLVQF SDTPETEFYL NTYQSKSDLL ARLSQLQLKG GSTLNIGSAL DFVLSNHFTE
AGGSRINEHV PQLLLLLTAG RSADSYLPAS NALARAGVLT FSVGTSAADQ AELEQIAFNP
SQAYLMDDFS SLPALPQQLI QPLTEMISGG VEEVPLAPTE TKRDILFLFD GSANLVGQFP
VVRDFLYKII DQLNVKPDGT RVAVAQYSDN VKVESRFADH QQKAEILGVV RKMKIKTGKT
LNVGAALDYA RRNIFVKSAG SRIDEGVLQF LVLLVAGRSA DSVAQPSDYL RRTGVVPFIF
QARNADPTEL QQIVLAPEFI LAAESLPKIG ELHPQIVNLL KSVQNGGQPQ GEKKDVVFLI
DGSDGVRTGF PLMKEFLQRV VESLDVGPDR VRVGVVQYCE RARPEFYLNT YNDQQSVVNG
IRSLAHMGGS TLNTGAALNF VLRNIFTAPA GSRITEGVPQ FLILLTADRS QDDVRGPSVV
LKRSGMVPFG IGIGKADIIE MKTISYVPDF ALSIPAFRDL NSIQQVISER VSQLTREELE
KLEPDVTFSQ ILPGSKRDIV FLIDGSQTAR PEFTYIRSFI ERLIENLDVG FDTTRVAVVQ
FSEDPKVEFL LNAHSSKDEM QSAVRRISPK GGRQINTGTA LEYVSKNIFD RALGSRIEEG
VPQFLILFSS GNADDDVEEP AGHVKQVGVA PLTIGKNIDP EELVKISLSP EYVFSVSTFR
ELPSLEQKLL TPITTLTSEQ IERILSSTQL PPPVVESDAA DIVFLIDSSD SVKPDGLAHI
RDFISSIVRK LNIGPSRVRI GVVQFSNDVF PEFYLKSHKT QSAVLDALRR LRFKGGSPLY
TSKALDFVAK NLFVKSAGSR IEDGVPQHLV LVLGGKSQDD VTRPSRVLGS AGIVRIGVGS
RNANRSELQA ITNDQKYVFT VRDFRDLSLL ESRIINSFGP SQATPPPHPP HPTPLPDKKK
ADIVFLLDGS INFKRDHFQE VLNFVSGIVD TVYEDGDSIQ VGLVQYNSDP TDEFFLKDFT
NKEQIMDAIS KVVYKGGRHA NTKVAIEHLT RHHFVPDAGS RLDQRVPQIA FIITGGKSIE
DAQEASMALS GKRVKVFAVG VKDIDSTEVS GIASNSATAF RVSTVQELSE LSEQVLETLH
DAMNEALCPG VPDVSRACNL DVILGFDGSA GQGVLESRVK NILDRITQMQ KISCTSNQEP
TVRVSIMANS ASGPVEAFDF SEYQPELFEK FQLLLGQRPY ILTADTLKAY QDKFRKSPAD
SVKVVIHFTD GTDENFARLE AASAALQQSG VNALIFVNLE HRDTNFDNVM ELEFGRGFTY
NRPLKLSLVD LDYELAEQLD SIAERACCGV PCKCSGQRGD RGVLGNIGQK GVPGEGGYRG
YPGDEGGPGE RGPPGLNGTQ GFQGCPGHRG TKVWSLSRSL QSRAHTLFSF QGEPGEPGPK
GGNGFRGPRG ETVSSLCLET NKSLISSLLT KENDLEKHPF STGPKECPVY PTELAFALDT
SAGVNQDAFR RMREVLLRIV ENLTIAESNC PRGARVAVVT YNNEVTTEVR FADSKRKSVL
LQKIQNLQGA FTSKQRSLET VMSFVARNTF KRARSGFLMR KVAVFFTNGP TKASPQLNEA
ILKLYDEGIT PLFLTNREDR TLKNALQINN TAVGDAIILT SRDYSETLKK ILTCHICLDI
CDPHESCGFG GQRLSFRDRR SAGTNVDLDV AFILDSSDTT TPFQFNEMKK YIAYTVKQLE
LSPNPKSSHL LARVAVLQHA PYEYERNSST LPVKVELSLT DYGSRDKLVD FLSNKMTQLH
GTRALGSAID FTIETVFESV PNPRDLKVLI LMLTGEVKKQ ELESLQRVII DAKCKGYFFV
ILGIGRKVNV KDIYSLSSEP NDVFFKLADK PTELNEETLL RFSRLLPSFI SSENAFYLSP
DIRKQCDWFQ GDQPAKNPVK FGQKQLHVPN NVTSSITTKP VSTTTKPVST TTKPVSTTMK
PVSTTTKPVS TTVKPVSATT KTVSITAKSV DPKTVEAKSG ATKSAGVKQV AAKPTDPKLV
DSKPVDPKTT VTKAASPKTA AAKQVTTKSG SREIQVFDIT ENSAKLQWVN PEPSSPYIYD
ITITSAHDHS LVLKQNITST ERVIGGLRTG QKYQVVITGY LKSQARISYA GSFTTTQSSP
PPPAPPKSAS TSTVNLMVNT EPLADLTDPC LLDFDMEGTC RKFILKWYYD SETKSCARFW
YGGCGGNENR FNTQKECEKV CIPALITVLC T
//
