ID K7G1A3_PELSI Unreviewed; 1562 AA.
AC K7G1A3;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=Tenascin R {ECO:0000313|Ensembl:ENSPSIP00000014063.1};
GN Name=TNR {ECO:0000313|Ensembl:ENSPSIP00000014063.1};
OS Pelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Trionychia;
OC Trionychidae; Pelodiscus.
OX NCBI_TaxID=13735 {ECO:0000313|Ensembl:ENSPSIP00000014063.1, ECO:0000313|Proteomes:UP000007267};
RN [1] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RG Soft-shell Turtle Genome Consortium;
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
RN [3] {ECO:0000313|Ensembl:ENSPSIP00000014063.1}
RP IDENTIFICATION.
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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; AGCU01203969; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01203970; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01203971; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01203972; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 13735.ENSPSIP00000014063; -.
DR Ensembl; ENSPSIT00000014128.1; ENSPSIP00000014063.1; ENSPSIG00000012294.1.
DR eggNOG; KOG1225; Eukaryota.
DR eggNOG; KOG2579; Eukaryota.
DR GeneTree; ENSGT00940000157761; -.
DR HOGENOM; CLU_001162_0_0_1; -.
DR OMA; QCVCDSD; -.
DR TreeFam; TF329915; -.
DR Proteomes; UP000007267; Unassembled WGS sequence.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0045121; C:membrane raft; IEA:Ensembl.
DR GO; GO:0072534; C:perineuronal net; IEA:Ensembl.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
DR GO; GO:0090733; C:tenascin complex; IEA:Ensembl.
DR GO; GO:0008306; P:associative learning; IEA:Ensembl.
DR GO; GO:0048677; P:axon extension involved in regeneration; IEA:Ensembl.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:Ensembl.
DR GO; GO:0035641; P:locomotory exploration behavior; IEA:Ensembl.
DR GO; GO:0060291; P:long-term synaptic potentiation; IEA:Ensembl.
DR GO; GO:0048692; P:negative regulation of axon extension involved in regeneration; IEA:Ensembl.
DR GO; GO:0022408; P:negative regulation of cell-cell adhesion; IEA:Ensembl.
DR GO; GO:0050805; P:negative regulation of synaptic transmission; IEA:Ensembl.
DR GO; GO:0097402; P:neuroblast migration; IEA:Ensembl.
DR GO; GO:0050885; P:neuromuscular process controlling balance; IEA:Ensembl.
DR GO; GO:0007158; P:neuron cell-cell adhesion; IEA:Ensembl.
DR GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; IEA:Ensembl.
DR GO; GO:0051971; P:positive regulation of transmission of nerve impulse; IEA:Ensembl.
DR GO; GO:0030334; P:regulation of cell migration; IEA:Ensembl.
DR GO; GO:0050808; P:synapse organization; IEA:Ensembl.
DR GO; GO:0035249; P:synaptic transmission, glutamatergic; IEA:Ensembl.
DR GO; GO:0022029; P:telencephalon cell migration; IEA:Ensembl.
DR CDD; cd00063; FN3; 10.
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; 10.
DR Gene3D; 2.10.25.10; Laminin; 3.
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; 2.
DR Pfam; PF00147; Fibrinogen_C; 1.
DR Pfam; PF00041; fn3; 10.
DR SMART; SM00181; EGF; 3.
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; 5.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 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, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Reference proteome {ECO:0000313|Proteomes:UP000007267};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022530}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..1562
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003902343"
FT DOMAIN 200..232
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 298..390
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 477..566
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 567..660
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 810..898
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 899..987
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 988..1078
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1079..1169
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1333..1548
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51406"
FT REGION 704..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 766..805
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 770..791
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 204..214
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 222..231
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1562 AA; 172697 MW; E383D75843E4957A CRC64;
MGADSENLAL RNLLIGLNLL LLGSVLKPFE CRLEVTTERT RRQVVDEEGN FANYSPPLKE
QSMVFNHVYN INVPLDSFCA SALEASSDQE VSAEDARMTE YTEQTSDTES QVTFTHRINL
PKQACKCFVS TQVMQELQSR IEMLEREVSV LRDQCNSNCC QENAATGQLD FVPHCSGHGN
FSLESCGCIC NEGWGGKNCS EPHCPLGCSS RGICVEDGEC VCEEGYAGED CSELRCPDDC
SGKGRCANGT CVCQEGYVGE GCAQLRCMNA CSGRGFCQEG LCACEEGYQG QDCSAVAPPE
ELRVAGIGDR SIDLEWDGPM AVTEYVISYQ PAVPGGLQLQ QQVPGDWSAI TLKELEPSLT
YNISIYAVIS DSLSTPVTTK VTTHLSTPRG LQFKTITETT VEVQWEPFSF SFDGWEISFI
PKVGTPETTA VSLLATQSQF DVTGLKPGEE YIVNVVALKE QARSPATSGS VSTLIDGPTQ
ILVRDVSDTV AFVEWTPPRA KVDYILLKYG LVNGEGGKTT FRLQPPLSQY SMQALRPGSR
YDVSISAVRG TNESDSAVTT FTTEIDAPKN LRVGLRTSAS LELEWDNSEA EVQTYKVVYS
TLAGEQYHEM LVPRSAGMTT RATLTDLVPG TEYGVGISAI MESKQSIPAT MNARTELDSP
RDLVVTASSE TSVSLAWTPA RGPIDHYRVT FIPASGMASE VTVPRDEAGA GTTSPPRSAP
TELDSPRDLV VTASSETSVS LAWTPARGPI DHYRVTFIPA SGMASEVTVP RDEAESEQRE
TSTRVWDRPS SRAHEQANSC SPTPPEWFRP ITQLHFSHVT SSSLNITWSD PSPPADRFLL
NYHPRDKEET TQVTLDASKR HAPLSGLQPS TEYIVSLVAV HGLVSSEPIV GSITTGIDPP
KNLTVGNITK DSVTLSWSPP EAAFDHYRVS YRSAQGRAES AAVANDVAEY TLRRLQPATR
HEISLSSVRG REESERISSV VYTAMDHPLG LSATNVTPTE ALLQWNPPLS KVESYVIVLA
PYTGQARGER KTVLVDGANQ EYQLINLMPS TSYMVTMYAT SGPLTSGTIS TNFTTLLDPP
TNLTASEVTR RSALLSWQPP MAPIENYIMT YRSPDGSRKE LIVDAEDTWI RLEGLSETTE
YTVRLQAAQD AMRSGFTATS FITGITLPSP CIGYTESENV LSMASPLREH INRYLIHCLS
SLYIEYHCVL SAIKDKSPTR SCVKKHRDYK IGVLCSWAKM KSLDSTFSDV KFTQALHPQR
KKLRPISYFV PICAVVQILL TYTAISGTVN LNKYHKRQRS HSLYPVELLS VKPLCLVVEG
LQAYGTMRLD TGGRVFANPQ DCAQHLMNGD TMSGIYTVSI NGDLTQRVQV YCDMTTDGGG
WIVFQRRQNG LTDFFRKWMD YRVGFGNLED EFWLGLENIH KITSQGRYEL RIDMRDGQEA
TYAYYDKFSL GDARSLYKLR IGDYNGTSGD SLTYHQGRPF STKDRDNDVA VTNCAMSYKG
AWWYKNCHRT NLNGKYGESR HSQGINWFHW KGHEFSIPFV EMKMRPYNHR NASGRKRRSL
QL
//
