ID A0A3B5QRQ7_XIPMA Unreviewed; 1285 AA.
AC A0A3B5QRQ7;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Tenascin R {ECO:0000313|Ensembl:ENSXMAP00000034039.1};
OS Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Xiphophorus.
OX NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000034039.1, ECO:0000313|Proteomes:UP000002852};
RN [1] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA Walter R., Schartl M., Warren W.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX PubMed=23542700; DOI=10.1038/ng.2604;
RA Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA Postlethwait J.H., Warren W.C.;
RT "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT evolutionary adaptation and several complex traits.";
RL Nat. Genet. 45:567-572(2013).
RN [3] {ECO:0000313|Ensembl:ENSXMAP00000034039.1}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000034039.1};
RG Ensembl;
RL Submitted (NOV-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 Ensembl; ENSXMAT00000022315.1; ENSXMAP00000034039.1; ENSXMAG00000015856.2.
DR GeneTree; ENSGT00940000157761; -.
DR Proteomes; UP000002852; Unassembled WGS sequence.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd00063; FN3; 8.
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; 8.
DR Gene3D; 2.10.25.10; Laminin; 4.
DR InterPro; IPR000742; EGF-like_dom.
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 NCBIfam; NF040941; GGGWT_bact; 1.
DR PANTHER; PTHR46708; TENASCIN; 1.
DR PANTHER; PTHR46708:SF6; TENASCIN-R; 1.
DR Pfam; PF18720; EGF_Tenascin; 3.
DR Pfam; PF00147; Fibrinogen_C; 1.
DR Pfam; PF00041; fn3; 8.
DR SMART; SM00181; EGF; 4.
DR SMART; SM00186; FBG; 1.
DR SMART; SM00060; FN3; 8.
DR SUPFAM; SSF56496; Fibrinogen C-terminal domain-like; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 5.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS00514; FIBRINOGEN_C_1; 1.
DR PROSITE; PS51406; FIBRINOGEN_C_2; 1.
DR PROSITE; PS50853; FN3; 7.
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:UP000002852};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022530}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..1285
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017280488"
FT DOMAIN 346..437
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 524..615
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 616..705
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 706..795
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 796..882
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 883..969
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 970..1064
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1056..1271
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51406"
FT REGION 97..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1285 AA; 141275 MW; C752658597B95E8F CRC64;
MPESKQLHWT TELTTMLALA LLFALQGAAH AAPSGDNKLV RTTRVRRQIP EGDQFPSASS
VNQTLREQPL VFNHVYNINV PMESLCSVDL DASVAPDSHA ELGSRPPVEG PGEPSGPTEY
TEQTLDAESQ VTFTHRINIP KAACSCPAIT TIQQLATRVE MLEREVSMLR AQCGSGCCGE
GSAIGRVDFV PGCSSHGSFS FDLCGCICEE GWGGKNCSEP RCPNDCSGQG VCIEGECVCD
RDFGGDNCSE PRCPSDCSGR GLCIDGECMC EESFTGEDCM VGRCLNDCSD QGMCVNGTCQ
CRPGYVGEDC SLVYCANNCS KKGVCKEGFC VCQDGFAGDD CNSVAPAMNL NARGVTDRTI
ELEWEGSIMV TDFLVTYTPS SPGGVQLEMR LPGNTTSWII TGLEAGIEYN INVFAVINNS
ISVPSSLTVW TYLSNPDGLV FKFITETSVE VQWQPFYYSF DGWEISFIPK DNDGGMTAQL
PSTITSFIQS GLRPGEEYTV NLVALREQGR SQPVTATFTT LIDGPTQLIV RDVSDTVAFV
EWTPPKAKID QIVLRYGLVR GEGPRTTFRL QPTLTQYSLQ VLRPGSRYEV SVSGVRKGNE
SGSISTEFTT EIDAPKNLRL VSKTSTTLEL EWDNSEAEVE GYQVVYSTLA GDQYDKVIVP
RNEGATTKTN LTDLLPGTEY GIGISAMKGI NQSTPATMNA RTGLDVPMDL TVTASTDNSI
TLVWGVVQGP IDHYRVTYTS SSGITTELTV PKDITTTTLT DLDPGTEYTI TVAARRGRQQ
STAATIDAFT EMDPPKELAV SDVTEDSVTI SWIKPLAPFE YYKLSYQSAR GRVDSEMIDS
DVTNYTLSSL FPATEYEISL NAVRGSQESR PVTTSVFTAM DMPAELTALN ITPQGALLRW
TPPLSNVDNY VLTITHNQLT ADTFLVEGNK HEHQLSNLKP STTYSVALYA TKGPLTSGTV
ITNLQTPMDA PVNLTASEVN HRSGLISWQP PIAEIDNYML TYKTPDGSRK ELILDAEDTW
IRLEGLAESA EYTVKLQAAR GLDTSAVVST TFTTGSRLFS TPQNCAQHLL NGETVSGVYT
IYINRDPSQG VQVYCDMTTD EGGWIVFQRR QNGLTDFSRK WSDYRVGFGN LEDEFWLGLD
NIQKIASQGR YELRIDMRDG QESVYANYDK FSIGDARNLY KLRIGEYNGT AGDSFSYHQG
RPFSTKDRDN DIAVTNCALS YKGAWWYKNC HRANLNGKYG ESRHSQGINW YHWKGHEFSI
PFVEMKMRPF NFRSISSKRR RSTTV
//
