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Database: UniProt
Entry: G1MFC7_AILME
LinkDB: G1MFC7_AILME
Original site: G1MFC7_AILME 
ID   G1MFC7_AILME            Unreviewed;      1358 AA.
AC   G1MFC7;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 2.
DT   27-MAR-2024, entry version 76.
DE   SubName: Full=Tenascin R {ECO:0000313|Ensembl:ENSAMEP00000018057.2};
GN   Name=TNR {ECO:0000313|Ensembl:ENSAMEP00000018057.2};
OS   Ailuropoda melanoleuca (Giant panda).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX   NCBI_TaxID=9646 {ECO:0000313|Ensembl:ENSAMEP00000018057.2, ECO:0000313|Proteomes:UP000008912};
RN   [1] {ECO:0000313|Ensembl:ENSAMEP00000018057.2, ECO:0000313|Proteomes:UP000008912}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=20010809; DOI=10.1038/nature08696;
RA   Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA   Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA   Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA   Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA   Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA   Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA   Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA   Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA   Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA   Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA   Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA   Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA   Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA   Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA   Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA   Wang J.;
RT   "The sequence and de novo assembly of the giant panda genome.";
RL   Nature 463:311-317(2010).
RN   [2] {ECO:0000313|Ensembl:ENSAMEP00000018057.2}
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}.
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DR   STRING; 9646.ENSAMEP00000018057; -.
DR   Ensembl; ENSAMET00000018788.2; ENSAMEP00000018057.2; ENSAMEG00000017071.2.
DR   Ensembl; ENSAMET00000037363.1; ENSAMEP00000030457.1; ENSAMEG00000017071.2.
DR   eggNOG; KOG1225; Eukaryota.
DR   eggNOG; KOG2579; Eukaryota.
DR   GeneTree; ENSGT00940000157761; -.
DR   HOGENOM; CLU_001162_0_0_1; -.
DR   TreeFam; TF329915; -.
DR   Proteomes; UP000008912; 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; 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; 4.
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; 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; PF07974; EGF_2; 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; 5.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS51406; FIBRINOGEN_C_2; 1.
DR   PROSITE; PS50853; FN3; 8.
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:UP000008912};
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..1358
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5041197549"
FT   DOMAIN          328..420
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          506..597
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          598..687
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          688..777
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          778..865
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          866..955
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          956..1042
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1043..1130
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1129..1344
FT                   /note="Fibrinogen C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51406"
SQ   SEQUENCE   1358 AA;  149062 MW;  8B6E736F7668F494 CRC64;
     MGVDGETVVL KSMLIGVNLI LLGSLLKPSQ CQLEVTTERV RRQAVEEEGG VANYSASGKE
     RPMVFNHVYN INVPLDSLCS SGLEASAERE VSAEDEALAE YTGQTSDHDS QVTFTHRINL
     PKKACPCAGS ARVLQELLSR IEMLEREVSL LRDQCASNCC PESAATGQLD YIPHCSGHGN
     FSLQSCGCIC NEGWFGKNCS EPYCPLGCSS RGVCVDGQCV CDSEYSGGDC SELRCPTDCS
     SRGLCVDGEC VCEEPYTGED CSKLRCPGDC SGKGRCANGT CFCQEGYVGD DCSQRRCPNA
     CSGRGHCQEG LCFCEDGYQG PDCSAVAPPE DLRVAGISDR SIELEWDGPL AVTEYVISYQ
     PTALGGLQLQ QRVPGDWTGV TITELEPGLT YNISVRSVIS SILSLPITAK VATHLSTPQG
     LHFKTITETT VEVQWEPFSF SFDGWEISFI PKNNEGGVIA QLPSDVTSFN QTGLKPGEEY
     IVNVVALKEQ ARSPPTSASV STVIDGPTQI LVRDVSDTVA FVEWTPPRAK VDFILLKYGL
     VGGEGGKTTF RLQPPLSQYS VQALRPGSRY EVWVSAVRGT NESQSTTTQF TTEIDAPKNL
     RVGSHTATSL DLEWDNSEAG VQEYKVVYST LAGEQYHELL VPKSIGPTTR ATLTDLVPGT
     EYGVGISAVM NSQQSVPATM NARTELDSPR DLMVTASSET SISLIWTKAS GPIDHYRITF
     TPSSGIASEV TVPKDRTSYT LTDLEPGAEY IISITAERGR QQSFESTVDA FTGFRPISHL
     HFSHVTSSSV NITWSDPSPP ADRLILNYSP RDEEEEMTEV SLDATKRHTV LMGLQPATEY
     IVNLVAVHGT VTSEPIVGSI TTGIDPPKDI TISNVTKDSV MVSWSPPVAS FDYYRVSYRP
     TQVGRLDSSV VPNTVTEFTI TKLYPATEYE ISLNSVRGRE ESERVCTLIH TAMDNPLDLT
     ATNITPTEAL LQWKAPVGGV ENYVIILTHF AVAGETILVD GGSEEFQLVG LLPSTHYTVN
     MYATSGPLTS GTVSTNFSTL LDPPANLTAS EVTRQSALIS WQPPRAEIEN YILTYKSTDG
     SRKELIVDAE DTWIRLEGLL ESTDYTVLLQ AAQDTSRSGL TSATFTTGGR VFPHPQDCAQ
     HLMNGDTLSG VYTIFLNGEL SRKLQVYCDM TTDGGGWIVF QRRQNGQTDF FRKWAEYRVG
     FGNLEDEFWL GLDNIHRITS QGRYELRVDM RDGQEAAFAY YDKFSVEDGR NLYKLRLGGY
     NGTAGDSLSY HQGRPFSTED RDNDVAVTNC AMSYKGAWWY KNCHRTNLNG KYGESRHSQG
     INWYHWKGHE FSIPFVEMKM RPYKHGLTAG RTRRSLRF
//
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