ID A0A2K6G041_PROCO Unreviewed; 3508 AA.
AC A0A2K6G041;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Tenascin XB {ECO:0000313|Ensembl:ENSPCOP00000019585.1};
GN Name=TNXB {ECO:0000313|Ensembl:ENSPCOP00000019585.1};
OS Propithecus coquereli (Coquerel's sifaka) (Propithecus verreauxi
OS coquereli).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC Indriidae; Propithecus.
OX NCBI_TaxID=379532 {ECO:0000313|Ensembl:ENSPCOP00000019585.1, ECO:0000313|Proteomes:UP000233160};
RN [1] {ECO:0000313|Ensembl:ENSPCOP00000019585.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
CC -!- SIMILARITY: Belongs to the tenascin family.
CC {ECO:0000256|ARBA:ARBA00008673}.
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DR STRING; 379532.ENSPCOP00000019585; -.
DR Ensembl; ENSPCOT00000030235.1; ENSPCOP00000019585.1; ENSPCOG00000021738.1.
DR GeneTree; ENSGT00940000155565; -.
DR Proteomes; UP000233160; Unplaced.
DR GO; GO:0031012; C:extracellular matrix; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:Ensembl.
DR GO; GO:0005518; F:collagen binding; IEA:Ensembl.
DR GO; GO:0098633; F:collagen fibril binding; IEA:Ensembl.
DR GO; GO:0008201; F:heparin binding; IEA:Ensembl.
DR GO; GO:0098609; P:cell-cell adhesion; IEA:Ensembl.
DR GO; GO:0007160; P:cell-matrix adhesion; IEA:Ensembl.
DR GO; GO:0030199; P:collagen fibril organization; IEA:Ensembl.
DR GO; GO:0032963; P:collagen metabolic process; IEA:Ensembl.
DR GO; GO:0048251; P:elastic fiber assembly; IEA:Ensembl.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:Ensembl.
DR GO; GO:1904028; P:positive regulation of collagen fibril organization; IEA:Ensembl.
DR GO; GO:0006641; P:triglyceride metabolic process; IEA:Ensembl.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd00063; FN3; 20.
DR CDD; cd00087; FReD; 1.
DR Gene3D; 3.90.215.10; Gamma Fibrinogen, chain A, domain 1; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 22.
DR Gene3D; 2.10.25.10; Laminin; 17.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR013111; EGF_extracell.
DR InterPro; IPR041161; EGF_Tenascin.
DR InterPro; IPR036056; Fibrinogen-like_C.
DR InterPro; IPR014716; Fibrinogen_a/b/g_C_1.
DR InterPro; IPR002181; Fibrinogen_a/b/g_C_dom.
DR InterPro; IPR020837; Fibrinogen_CS.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR46708; TENASCIN; 1.
DR PANTHER; PTHR46708:SF3; TENASCIN-X; 1.
DR Pfam; PF07974; EGF_2; 5.
DR Pfam; PF18720; EGF_Tenascin; 9.
DR Pfam; PF00147; Fibrinogen_C; 1.
DR Pfam; PF00041; fn3; 19.
DR SMART; SM00181; EGF; 18.
DR SMART; SM00186; FBG; 1.
DR SMART; SM00060; FN3; 23.
DR SUPFAM; SSF56496; Fibrinogen C-terminal domain-like; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 20.
DR PROSITE; PS00022; EGF_1; 8.
DR PROSITE; PS01186; EGF_2; 8.
DR PROSITE; PS00514; FIBRINOGEN_C_1; 1.
DR PROSITE; PS51406; FIBRINOGEN_C_2; 1.
DR PROSITE; PS50853; FN3; 19.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Reference proteome {ECO:0000313|Proteomes:UP000233160};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022530}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..3508
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014356440"
FT DOMAIN 749..839
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 840..930
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1062..1153
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1157..1247
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1261..1350
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1367..1467
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1475..1565
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1578..1667
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1673..1763
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1776..1865
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1881..1969
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 2307..2402
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 2501..2591
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 2602..2692
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 2817..2911
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 2921..3018
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 3022..3111
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 3112..3198
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 3199..3288
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 3285..3500
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51406"
FT REGION 27..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 918..955
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1048..1067
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1236..1260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1340..1387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1966..1991
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2051..2088
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2457..2502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2576..2606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2801..2821
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2898..2922
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 939..953
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1243..1257
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2058..2075
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3508 AA; 378782 MW; 8CFDE489BF4E7989 CRC64;
MMPAQHPLTS CLAVLVLLGT ARAGPFSSRS NVTLSAPRPP PQPGGRTVGT GGGSPSSQLY
EHTMEGGEKQ VVFTHRINLP PSAGCGCPPG TEPPVPASEV QALRVRLEIL EELVKGLKEQ
CTGGCCPAAA QAGTGQTDVR SLCSLHGVFD LSRCACSCEP GWGGPTCSDP KDPGMSPSSP
PSGSCPDDCN DQGRCVRGRC VCFPGYTGPS CGWPSCPGDC QGRGRCVQGV CVCRAGFSGA
DCGQRSCPRG CSQRGRCEDG RCVCDPGYAG EDCGMRSCPR GCSQRGRCED GRCVCDPGYT
GEDCGQRSCP RGCSQRGRCE NGRCVCDPGY SGEDCGVRSC PWDCGEGGRC VDGRCVCWPG
YAGEDCSTRT CPRDCRGRGR CEDGECICDA GYSGDDCGVR SCPGDCNQRG RCEDGRCVCW
PGYTGPDCGA RACPRDCRGR GRCENGVCVC NAGYSGEDCG VRSCPGDCRG RGRCESGRCL
CWPGYTGRDC GTRACPGDCR GRGRCVDGRC VCNPGFAGED CGSRRCPGDC RGHGRCEEGV
CVCDAGYSGE DCSARSCPGG CRGRGQCVDG RCECDDEYSG EDCGVRRCPR DCSQHGVCQD
GVCICWEGYV GEDCSVRTCP SNCHGRGRCE DGRCVCNPGY TGPACATRSC PADCRGRGRC
VQGVCVCHAG YGGEDCGQEE PPASACPGGC GPRELCQAGQ CVCVEGFRGP DCAIQTCPGD
CRGRGECRQG SCVCQDGYAG EDCGEEVPAI EGMRMHLLEE TTVRTEWTRA PGPVDAYEIQ
FIPTTEGASP PFTARVPSSA SAYDQRGLAP GQEYQVTVRA LRGTSWGPPA SKTITTMIDG
PQDLRVVAVT PTTLELSWLR PQAEVDRFVV SYVSAGNQRV RLEVPPEADR TLLTDLMPGV
EYVVTVTAER GRAVSYPTSV RANTGSSPSG LLGATDEPPP SGPSTTQGAR APLLQQRPQE
LGELRVLGRD KTGHLHVAWT AQPDTFAHFQ LRLRVPEGPG AHEELLPGDV RQALVPPPPL
GAPYELSLRG VPPGGKPSDP IIYQGIMDRD EEKPGKPSGP PRLGELTATD MTSDSLLLRW
TVPEGEFDSF VIQYKDRDGQ PQVLPVEGPQ RSAPITSLDP GRKYKFVLYG LVGKKRHGPL
VAEAKILPRS DPSPGTPPRL GKLWVTDPTP DSLHLSWTVP EGQFDSFMVQ YRDRDGRPQV
VPVEGPERSV VISPLDPDHK YRFTLFGIAN KKRYGPLTAD GTTAPERKEE HPRPESPEQP
LLGELTVTGV TPDSLRLSWT VAQGPFDSFM VQYKDAQGQP QAVPVKGDEN EVTVPGLEPD
RKYKMNLYGL RGRQRVGPVS VVAKTAPQES VEETPSPTEP STEAPEPPEE PLLGELTVTG
SSPDSLSLSW TVPQGHFDSF TVQYKDRDGR PQVVRVRGEE REMTVGGLEP GRKYKMHLYG
LHEGQRVGPA STVGVTAPQW EEETPPATQP PPEPRLGELT VTDVTPNSVG LLWTVPEGHF
DSFVVQYKDS DGQPQVVPVA ADQREVTVSN LEPARKYKMN FYGLHGRQRV GPLSVVAVTD
PLPPAPATEA SKLLLEPRLG ELAVVDVTPD SVDLSWTVPE GEFDSFVVQY KDRDGQPQVM
PVAADQREVT VPGLEPSRKY KFLLFGIRDG KRRSPVSVEA KTAARGDASP GAPPQLGELW
VTDPTSDSLR LSWTVPEGQF DSFVVQFKDK DGPRVVPVEG HERSVAVAPL DPGRKYRFLL
YGLLGKKRHG PLTAEGTTEA WSAVDTGTKH PPKPRLGEEL QVTSVTPNSV GLSWTVPEGQ
FDSFVVQYKD RAGQPQVVPV EGSLREVGIS DLDPAHRYKL LLYGLHGGKR VGPISAIAMT
APREEIEAET AAPTPSASEP HLGELTVGEA TPHTLQLSWV VTQGEFDSFE VQYTDREGRL
QVVDVGGDQN DITLSGLESD HRYLVTLYGF HDGRRVGPAH IEALTVPQEE EDEPSEPPTT
TPEPPIKPRL GELTVTDATP DSLSLTWTVP EGQFDHFLAV RVGGEEREMT VGGLEPGRKY
KMHLYGLHEG RRVGPTSTVG VTAPQDVDET PSPTEPSTEA PEPPEEPLLG ELTVTGSSPD
SLNSLSLTWT VPEGQFDHFL VQYKNGDGQP KVVRVPGHED GVTGPFDSFV VQYRDAQGQP
QAVPVSRDLR EVTILGLDPA RKYKFLLFGL QDGKRHGPLD VHVSEPRPVY LLGRLKPRPS
APLPPHSHPS PYAPTPQGTL AFLPGSSFIP TPGPVTPPER EVTVGGLEPG RKYKMHLYGL
HEGRRVGPAS TVGVTGEWET AALPTRPPVE PRLGELAVAE VTSDSVRLWW TVAQGPFDSF
VVQYRDAQGQ PQAVPVSRDL REVTILGLDP ARKYKFLLFG LQDGKRHGPV PVEAKTGERG
PGSPLPARAP LWRQLDVHAL SSPSPSLPSF SLRSHAPGDT CFLAWLLLHP DSWPSHPSCS
LDQLAEPQQP RKPSGPSAPS LSHPLCTSLP FPAPDTKPSP RLGELAVADV TPDSVDLSWT
VPAGEFDSFV VQYKDRDGQP QVVPVAADQR EVTVPGLEPS RKYKFLLYGL AGRKRLGPSS
AEATTGEPRP SPREEEPQPP PRLGELTVDE ETSDSLRLLW TVAQGPFDSF VVQYRDKNGQ
PQVVPVAADQ RKVTIGDLEP GRKYKFLLYG LLRGKRLGPV SVLGMTGETV LLSSSESSAA
AARETGRSVG LRGPGVQESM PRLRRGKILE DRRSLLSLQM AAMARTCRVP PQPWGNPTTP
SLGSMVAHIC SPSYLGGKGG RITRGQGLGN IARPSSPLAF SHVAPEEDTP APETPEPPEE
PRLGVLAVTD TAPDSIRLSW NVARGPFDSF VVQYEDTDGQ PQALLVDGDQ SKVLISGLEP
STPYKFFLYG LREGKRLGPV STEGTTGPAP AGQIPGEPGP RLSQLSVTDV TTSSLRLNWE
APPEAFDSFL LRFGVPSPST LEPHPRPLLQ RELVVPGTRR SAVLRDLRPG TLYSLTLYGL
RGPHKADSIQ GTARTLSPVL ESPRDLQFSE IGETSAKVSW MPPSSRVDSF KVSYQLADGG
EPQSVQVDGR ARTQTLQGLI PGARYEVTVV SVRGFEESEP LTGFLTTVPD GPTQLRALNL
TEDSALLHWK PPQNPVDTYD VRVTAPGAPS LQGSAPGSAE DYPLHRLVLH TNYTATVQGL
RGPNLTSPAS ITFTTGLEAP QDLEAKEVTP RTALLTWTEP PVPPTGYLLS FDTPGGQTQE
ILLPRGVTSH RLLGLFPSTP YSARLRAMWG ESLTPPVSTS FTTGALRIPF PRDCGEEMQN
GASTSRTTTI FLNGNRERPL NVFCDLETDG GGWLVFQRRM DGQTDFWRDW EEYAHGFGNI
SGEFWLGNEA LHSLTKAGDY SMRVDLRAGD EAVFAQYDSF RVDSAAEYYR LHLEGYHGTA
GDSMSYHSGS VFSARDRDPN NLLISCAVSY RGAWWYRNCH YANLNGLYGS TVDHQGVSWY
SWKGFEFSVP FTEMKLRPRS FRSPAGGG
//
