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Database: UniProt/TrEMBL
Entry: A9JRJ1_XENTR
LinkDB: A9JRJ1_XENTR
Original site: A9JRJ1_XENTR 
ID   A9JRJ1_XENTR            Unreviewed;      1350 AA.
AC   A9JRJ1;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 95.
DE   SubName: Full=LOC100135076 protein {ECO:0000313|EMBL:AAI55682.1};
DE   SubName: Full=Tenascin-R precursor {ECO:0000313|RefSeq:NP_001107287.1};
GN   Name=tnr {ECO:0000313|RefSeq:NP_001107287.1,
GN   ECO:0000313|Xenbase:XB-GENE-948286};
GN   Synonyms=janusi {ECO:0000313|RefSeq:NP_001107287.1}, LOC100135076
GN   {ECO:0000313|EMBL:AAI55682.1}, restrictin
GN   {ECO:0000313|RefSeq:NP_001107287.1}, tenascin-r
GN   {ECO:0000313|RefSeq:NP_001107287.1}, xtnr
GN   {ECO:0000313|RefSeq:NP_001107287.1};
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364 {ECO:0000313|EMBL:AAI55682.1};
RN   [1] {ECO:0000313|RefSeq:NP_001107287.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=12454917; DOI=10.1002/dvdy.10174;
RA   Klein S.L., Strausberg R.L., Wagner L., Pontius J., Clifton S.W.,
RA   Richardson P.;
RT   "Genetic and genomic tools for Xenopus research: The NIH Xenopus
RT   initiative.";
RL   Dev. Dyn. 225:384-391(2002).
RN   [2] {ECO:0000313|EMBL:AAI55682.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain {ECO:0000313|EMBL:AAI55682.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|RefSeq:NP_001107287.1}
RP   IDENTIFICATION.
RG   RefSeq;
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   EMBL; BC155681; AAI55682.1; -; mRNA.
DR   RefSeq; NP_001107287.1; NM_001113815.1.
DR   GeneID; 100135076; -.
DR   KEGG; xtr:100135076; -.
DR   AGR; Xenbase:XB-GENE-948286; -.
DR   CTD; 7143; -.
DR   Xenbase; XB-GENE-948286; tnr.
DR   OMA; QCVCDSD; -.
DR   OrthoDB; 5489847at2759; -.
DR   Proteomes; UP000008143; Chromosome 4.
DR   CDD; cd00063; FN3; 9.
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; 9.
DR   Gene3D; 2.10.25.10; Laminin; 5.
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; 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; 9.
DR   SMART; SM00181; EGF; 4.
DR   SMART; SM00186; FBG; 1.
DR   SMART; SM00060; FN3; 9.
DR   SUPFAM; SSF56496; Fibrinogen C-terminal domain-like; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 6.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS51406; FIBRINOGEN_C_2; 1.
DR   PROSITE; PS50853; FN3; 9.
PE   2: Evidence at transcript level;
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:UP000008143};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Secreted {ECO:0000256|ARBA:ARBA00022530};
KW   Signal {ECO:0000256|SAM:SignalP, ECO:0000313|RefSeq:NP_001107287.1}.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           32..1350
FT                   /evidence="ECO:0000256|SAM:SignalP,
FT                   ECO:0000313|RefSeq:NP_001107287.1"
FT                   /id="PRO_5033207420"
FT   DOMAIN          321..413
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          414..504
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          505..592
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          593..684
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          685..774
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          775..861
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          862..951
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          952..1037
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1038..1125
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1124..1339
FT                   /note="Fibrinogen C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51406"
SQ   SEQUENCE   1350 AA;  149693 MW;  753F62B914BC016B CRC64;
     MGSEGVSSAL GPLQVGVHLI LLACLTRRSQ CQSELTGQTP RLDIQVDKGG NMTDHGIENK
     QNPMVFNHVY NFNVPLSFPC TLEPETPEDG SWVTQQTENT ADAGSQITFT HSIRVPQRLC
     QCYTTPHAVQ HLLSRIEALE REVMLLRERC NDRACQDAEA TGLTEFAPPC SGHGNFTVDS
     CICNQGWGGE NCSEPLCPLE CSGRGTCIEG MCVCEPDYTG EWCTDLLCPE ECSPHGLCQD
     GQCVCQDPYI GIGCTELRCP GDCLGKGRCA NGTCVCQDGY AGEDCGRMWC INACSGRGQC
     QDGVCECEEG YSGQDCSEVA PPVDFSVTAV GDHWMDLAWE GTTAVTEYVI SYQPAVPGEW
     GTQQRLQQRV PGDWSSVTIR ELEPGVTYNI SVCSVISDII SEPASITIST HISSPRGLNF
     MEVTQTSVEV HWDPPVFPLD GWEISFTPKN NEGGLTVQLP SSVTSFNQTG LKPGEEYTVS
     IISLKDQARS PATSGSISTD IDGPTNILVR DVTDTVAFVE WTPARAKLDF MQLDYGPING
     EGEKTTFRLQ PPLSQYSMQV LRPGSQYEIS IRGVRGDTES EPVRATFTTE LDAPKNLRVI
     SHASSTLELE WDNSEAEGEG YRVVYSTLAG DQYHELIVPR NYGQTTKATL TDLIPGTEYG
     IGISAIRYNL KSAPATMNAR TELDSPTDLM VTGSTDKSIS LTWTKARGPI DHYRISFTPS
     SGMASEVTVP SDISQYELSE LEPGTEYTIS IFAERGRQQS KETTIDAFTG FRPITQLHFS
     AVTAYSVNVS WTDPSPPPDQ FILTYNPIDS KDPLQLFLDP SLRQTRLSAL QPSTEYMVTL
     LPVHGTVRAE LVEGTVTTGV APPMDLSVIN VTENSLAVVW RPPPSSLHHY RLTYQSTKGR
     MDSVVIGNDQ TRYTLANLMP NTEYKISLRS VRGREESERV GIVSWTAVDP PYGLRTSNIT
     ATEALLHWEP PRSEVESYVI IVTHHAGSGE TILVDGESIE FQLQNLLPRT NYSVTLSANF
     GHQTSRSVGV SFTTILDPPM NLTATEVART SALISWQPPI SPIENYILTY KSANESRKEL
     IVDAEDTWIR LEGLLESTEY TVSILSVQNG ERSSVTHTVF TTGGRVFSYP QDCAQHMLNG
     DNQSGVYYIY INGDMSQSVP VYCDMATDAG GWIVFQRRQN GLTDFFRKWA DYRVGFGNLE
     DEFWLGLDTL HQVTSQGRYE LRIDMRDGQE AVYAYYNKFN IGDARSLYKL RIGDFNGTSG
     DSLTYHQGRP FSTKDRDNDV AVTNCASSYK GAWWYKNCHR TNLNGKYGES RHSQGINWYH
     WKGHEFSIPF VEMKMRPYNH RTMKKRSLQL
//
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