TENA_PIG
ID TENA_PIG Reviewed; 1746 AA.
AC Q29116; P98142;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 145.
DE RecName: Full=Tenascin;
DE Short=TN;
DE AltName: Full=Cytotactin;
DE AltName: Full=GMEM;
DE AltName: Full=GP 150-225;
DE AltName: Full=Glioma-associated-extracellular matrix antigen;
DE AltName: Full=Hexabrachion;
DE AltName: Full=JI;
DE AltName: Full=Myotendinous antigen;
DE AltName: Full=Neuronectin;
DE AltName: Full=P230;
DE AltName: Full=Tenascin-C;
DE Short=TN-C;
DE Flags: Precursor;
GN Name=TNC; Synonyms=HXB;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS MAJOR; MINOR-1 AND MINOR-2).
RC TISSUE=Submandibular gland;
RX PubMed=1722152; DOI=10.1111/j.1432-1033.1991.tb16418.x;
RA Nishi T., Weinstein J., Gillespie W.M., Paulson J.C.;
RT "Complete primary structure of porcine tenascin. Detection of tenascin
RT transcript in adult submaxillary glands.";
RL Eur. J. Biochem. 202:643-648(1991).
RN [2]
RP PROTEIN SEQUENCE OF 813-825; 887-917; 998-1011; 1597-1608 AND 1719-1730.
RC TISSUE=Fetal brain;
RX PubMed=9498558; DOI=10.1093/oxfordjournals.jbchem.a021874;
RA Wakatsuki S., Ho S.H., Arioka M., Yamasaki M., Kitamoto K.;
RT "Isolation and characterization of a 230 kDa protein (p230) specifically
RT expressed in fetal brains: its involvement in neurite outgrowth from rat
RT cerebral cortex neurons grown on monolayer of astrocytes.";
RL J. Biochem. 122:1146-1152(1997).
CC -!- FUNCTION: Extracellular matrix protein implicated in guidance of
CC migrating neurons as well as axons during development, synaptic
CC plasticity as well as neuronal regeneration. Promotes neurite outgrowth
CC from cortical neurons grown on a monolayer of astrocytes. Ligand for
CC integrins alpha-8/beta-1, alpha-9/beta-1, alpha-V/beta-3 and alpha-
CC V/beta-6. In tumors, stimulates angiogenesis by elongation, migration
CC and sprouting of endothelial cells (By similarity).
CC {ECO:0000250|UniProtKB:P24821}.
CC -!- SUBUNIT: Homohexamer; disulfide-linked. A homotrimer may be formed in
CC the triple coiled-coil region and may be stabilized by disulfide rings
CC at both ends. Two of such half-hexabrachions may be disulfide linked
CC within the central globule. Interacts with CSPG4 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Isoforms are produced in a tissue- and time-specific manner
CC during development.;
CC Name=Minor-2;
CC IsoId=Q29116-1; Sequence=Displayed;
CC Name=Major;
CC IsoId=Q29116-2; Sequence=VSP_001416;
CC Name=Minor-1;
CC IsoId=Q29116-3; Sequence=VSP_001417;
CC -!- TISSUE SPECIFICITY: Submaxillary glands and brain.
CC -!- DEVELOPMENTAL STAGE: Predominantly expressed in the embryonic and early
CC postnatal stages. Little or no detection in adult brain.
CC -!- INDUCTION: By TGF-beta.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the tenascin family. {ECO:0000305}.
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DR EMBL; X61599; CAA43796.1; -; mRNA.
DR PIR; S19694; S19694.
DR RefSeq; NP_999395.1; NM_214230.1.
DR AlphaFoldDB; Q29116; -.
DR SMR; Q29116; -.
DR STRING; 9823.ENSSSCP00000005891; -.
DR PaxDb; Q29116; -.
DR PeptideAtlas; Q29116; -.
DR PRIDE; Q29116; -.
DR GeneID; 397460; -.
DR KEGG; ssc:397460; -.
DR CTD; 3371; -.
DR eggNOG; KOG1225; Eukaryota.
DR InParanoid; Q29116; -.
DR OrthoDB; 18592at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0042127; P:regulation of cell population proliferation; IEA:InterPro.
DR CDD; cd00063; FN3; 10.
DR CDD; cd00087; FReD; 1.
DR Gene3D; 2.60.40.10; -; 10.
DR Gene3D; 3.90.215.10; -; 1.
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 InterPro; IPR033078; TNC.
DR PANTHER; PTHR46708:SF1; PTHR46708:SF1; 4.
DR Pfam; PF07974; EGF_2; 3.
DR Pfam; PF18720; EGF_Tenascin; 10.
DR Pfam; PF00147; Fibrinogen_C; 1.
DR Pfam; PF00041; fn3; 10.
DR SMART; SM00181; EGF; 14.
DR SMART; SM00186; FBG; 1.
DR SMART; SM00060; FN3; 10.
DR SUPFAM; SSF49265; SSF49265; 7.
DR SUPFAM; SSF56496; SSF56496; 1.
DR PROSITE; PS00022; EGF_1; 15.
DR PROSITE; PS01186; EGF_2; 14.
DR PROSITE; PS50026; EGF_3; 5.
DR PROSITE; PS51406; FIBRINOGEN_C_2; 1.
DR PROSITE; PS50853; FN3; 9.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Coiled coil;
KW Direct protein sequencing; Disulfide bond; EGF-like domain;
KW Extracellular matrix; Glycoprotein; Phosphoprotein; Reference proteome;
KW Repeat; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..1746
FT /note="Tenascin"
FT /id="PRO_0000007742"
FT DOMAIN 174..186
FT /note="EGF-like 1; incomplete"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 187..217
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 218..249
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 250..280
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 281..311
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 312..342
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 343..373
FT /note="EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 374..404
FT /note="EGF-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 405..435
FT /note="EGF-like 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 436..466
FT /note="EGF-like 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 467..497
FT /note="EGF-like 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 498..528
FT /note="EGF-like 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 529..559
FT /note="EGF-like 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 560..589
FT /note="EGF-like 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 590..620
FT /note="EGF-like 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 625..717
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 718..801
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 805..894
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 895..988
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 989..1075
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1076..1166
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1167..1256
FT /note="Fibronectin type-III 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1257..1346
FT /note="Fibronectin type-III 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1347..1433
FT /note="Fibronectin type-III 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1434..1522
FT /note="Fibronectin type-III 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1520..1735
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT REGION 23..185
FT /note="Involved in hexamer formation"
FT COILED 118..145
FT /evidence="ECO:0000255"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P24821"
FT MOD_RES 70
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P24821"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P24821"
FT MOD_RES 905
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P24821"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 327
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 788
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1034
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1079
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1121
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1354
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 64
FT /note="Interchain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076,
FT ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 190..200
FT /evidence="ECO:0000250"
FT DISULFID 194..205
FT /evidence="ECO:0000250"
FT DISULFID 207..216
FT /evidence="ECO:0000250"
FT DISULFID 221..231
FT /evidence="ECO:0000250"
FT DISULFID 225..236
FT /evidence="ECO:0000250"
FT DISULFID 238..247
FT /evidence="ECO:0000250"
FT DISULFID 252..263
FT /evidence="ECO:0000250"
FT DISULFID 256..268
FT /evidence="ECO:0000250"
FT DISULFID 270..279
FT /evidence="ECO:0000250"
FT DISULFID 284..294
FT /evidence="ECO:0000250"
FT DISULFID 288..299
FT /evidence="ECO:0000250"
FT DISULFID 301..310
FT /evidence="ECO:0000250"
FT DISULFID 315..325
FT /evidence="ECO:0000250"
FT DISULFID 319..330
FT /evidence="ECO:0000250"
FT DISULFID 332..341
FT /evidence="ECO:0000250"
FT DISULFID 346..356
FT /evidence="ECO:0000250"
FT DISULFID 350..361
FT /evidence="ECO:0000250"
FT DISULFID 363..372
FT /evidence="ECO:0000250"
FT DISULFID 377..387
FT /evidence="ECO:0000250"
FT DISULFID 381..392
FT /evidence="ECO:0000250"
FT DISULFID 394..403
FT /evidence="ECO:0000250"
FT DISULFID 408..418
FT /evidence="ECO:0000250"
FT DISULFID 412..423
FT /evidence="ECO:0000250"
FT DISULFID 425..434
FT /evidence="ECO:0000250"
FT DISULFID 439..449
FT /evidence="ECO:0000250"
FT DISULFID 443..454
FT /evidence="ECO:0000250"
FT DISULFID 456..465
FT /evidence="ECO:0000250"
FT DISULFID 470..480
FT /evidence="ECO:0000250"
FT DISULFID 474..485
FT /evidence="ECO:0000250"
FT DISULFID 487..496
FT /evidence="ECO:0000250"
FT DISULFID 501..511
FT /evidence="ECO:0000250"
FT DISULFID 505..516
FT /evidence="ECO:0000250"
FT DISULFID 518..527
FT /evidence="ECO:0000250"
FT DISULFID 532..542
FT /evidence="ECO:0000250"
FT DISULFID 536..547
FT /evidence="ECO:0000250"
FT DISULFID 549..558
FT /evidence="ECO:0000250"
FT DISULFID 563..573
FT /evidence="ECO:0000250"
FT DISULFID 567..578
FT /evidence="ECO:0000250"
FT DISULFID 580..589
FT /evidence="ECO:0000250"
FT DISULFID 594..604
FT /evidence="ECO:0000250"
FT DISULFID 598..609
FT /evidence="ECO:0000250"
FT DISULFID 611..620
FT /evidence="ECO:0000250"
FT VAR_SEQ 1072..1253
FT /note="Missing (in isoform Minor-1)"
FT /evidence="ECO:0000303|PubMed:1722152"
FT /id="VSP_001417"
FT VAR_SEQ 1072..1162
FT /note="Missing (in isoform Major)"
FT /evidence="ECO:0000303|PubMed:1722152"
FT /id="VSP_001416"
FT CONFLICT 1007
FT /note="T -> M (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1746 AA; 191400 MW; 56549B1CFE5E5C88 CRC64;
MGVVTRLLVG TFLASLALPA QGGVLKKVIR HKRQTGVNVT LPEESQPVVF NHVYNIKLPV
GSQCSVDLES ASGDKDLAAP SEPSESVQEH TVDGENQIVF THRINIPRRA CGCAAAPDVK
ELLSRLEELE NLVSSLREQC TSGAGCCLQP AEGRLDTRPF CSGRGNFSTE GCGCVCEPGW
KGPNCSEPEC PSNCHLRGQC VDGQCVCNEG FTGEDCSQLA CPSDCNDQGK CVNGVCVCFE
GYSGVDCSRE TCPVPCSEEH GRCVDGRCVC QEGFAGEDCN EPLCLHNCHG RGRCVENECV
CDEGFTGEDC GELICPKDCF DRGRCINGTC YCDEGFEGED CGRLACPHGC RGRGRCEEGQ
CVCDEGFAGA DCSERRCPSD CHNRGRCLDG RCECDDGFEG EDCGELRCPG GCSGHGRCVN
GQCVCDEGRT GEDCSQLRCP NDCHGRGRCV QGRCECEHGF QGYDCSEMSC PHDCHQHGRC
VNGMCVCDDG YTGEDCRELR CPGDCSQRGR CVDGRCVCEH GFAGPDCADL ACPSDCHGRG
RCVNGQCVCH EGFTGKDCGQ RRCPGDCHGQ GRCVDGQCVC HEGFTGLDCG QRSCPNDCSN
WGQCVSGRCI CNEGYSGEDC SQVSPPKDLI VTEVTEETVN LAWDNEMRVT EYLIVYTPTH
EDGLEMQFRV PGDQTSTTIR ELEPGVEYFI RVFAILENKK SIPVSARVAT YLPTPEGLKF
KSIKETSVEV EWDPLDIAFE TWEIIFRNMN KEDEGEITKS LRRPETTYRQ TGLAPGQEYE
ISLHIVKNNT RGPGLKRVTT TRLDAPSQIE AKDVTDTTAL ITWFKPLAEI DGIELTYGIK
DVPGDRTTID LTHEENQYSI GNLKPDTEYE VSLISRRADM SSNPAKETFT TGLDAPRNLR
RISQTDNSIT LEWRNGKAAA DTYRIKYAPI SGGDHAEVEV PRSPQTTTKA TLTGLRPGTE
YGIGVSAVKG DKESDPATIN AATDLDPPKD FRVSELKESS LTLLWRTPLA KFDRYRLNYG
LPSGQPVEVQ LPRNATSYIL RGLEPGQEYT ILLTAEKGRH KSKPARVKAS TAGEPEIGNL
SVSDITPESF SLSWTATEGA FETFTIEIID SNRFLETMEY NISGAERTAH ISGLRPGNDF
IVYLSGLAPG IQTKPISATA TTEAEPEVDN LLVSDATPDG FRLSWTADEG VFDSFVLKIR
DTKKQSEPLE ITLLASERTR DITGLREATE YEIELYGISS GKRSQPVSAI ATTAMGSPKE
ITFSDITENS ATVSWMVPTA QVESFRITYV PITGGAPSVV TVDGTKTQTR LLRLLPGVEY
LVSVIAVKGF EESEPVSGTL TTALDGPSGL VTANITDSEA LAMWQPAIAP VDHYVISYTG
DRVPEITRTV SGNTVEYALT NLEPATEYTL RIFAEKGPQK SSTITTKFTT DLDSPRDLTA
TEVQSETALL TWRPPRASVT GYLLVYESVD GTLKEVVVGP ETTSYSLSGL SPSTHYTARI
QALNGPLRSK MSQTVFTTIG LLYPFPRDCS QAMLNGDTTS GLYTIYVNND KAQKLEVFCD
MTSDSGGWIV FLRRKNGRED FYRNWKAYAA GFGDLKEEFW LGLDALSKIT AQGQYELRVD
LRDHGETAYA VYDRFSVGDA RTRYKLKVEG YSGTAGDSMA YHNGRSFSTF DKDTDSAITN
CALSYKGAFW YKNCHRVNLM GRYGDNSHSQ GVNWFHWKGH EYSIQFAEMK LRPSNFRNLE
GRRKRA
