TEN1_CAEEL
ID TEN1_CAEEL Reviewed; 2684 AA.
AC G5EGQ6; B5BM17; Q5CCJ6;
DT 06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Teneurin-1;
GN Name=ten-1; ORFNames=R13F6.4;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, PROTEOLYTIC
RP PROCESSING, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RC STRAIN=Bristol;
RX PubMed=15936327; DOI=10.1016/j.ydbio.2005.02.017;
RA Drabikowski K., Trzebiatowska A., Chiquet-Ehrismann R.;
RT "ten-1, an essential gene for germ cell development, epidermal
RT morphogenesis, gonad migration, and neuronal pathfinding in Caenorhabditis
RT elegans.";
RL Dev. Biol. 282:27-38(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=18632986; DOI=10.1091/mbc.e08-01-0028;
RA Trzebiatowska A., Topf U., Sauder U., Drabikowski K., Chiquet-Ehrismann R.;
RT "Caenorhabditis elegans teneurin, ten-1, is required for gonadal and
RT pharyngeal basement membrane integrity and acts redundantly with integrin
RT ina-1 and dystroglycan dgn-1.";
RL Mol. Biol. Cell 19:3898-3908(2008).
RN [4]
RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=20497576; DOI=10.1186/1471-213x-10-55;
RA Morck C., Vivekanand V., Jafari G., Pilon M.;
RT "C. elegans ten-1 is synthetic lethal with mutations in cytoskeleton
RT regulators, and enhances many axon guidance defective mutants.";
RL BMC Dev. Biol. 10:55-55(2010).
CC -!- FUNCTION: Plays a role in the gonadal basement membrane maintenance
CC and/or adhesion early in development. Contributes to the guidance of
CC pharyngeal neurons. {ECO:0000269|PubMed:15936327,
CC ECO:0000269|PubMed:18632986, ECO:0000269|PubMed:20497576}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15936327}. Cell
CC membrane {ECO:0000269|PubMed:15936327}. Membrane {ECO:0000305}; Single-
CC pass membrane protein {ECO:0000305}. Note=Colocalizes in the nucleus
CC with a punctuate pattern.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=ten-1a, ten-1L;
CC IsoId=G5EGQ6-1; Sequence=Displayed;
CC Name=2; Synonyms=ten-1b, ten-1S;
CC IsoId=G5EGQ6-2; Sequence=VSP_045023;
CC -!- TISSUE SPECIFICITY: Isoform 1 is mainly expressed in organs derived
CC from the mesoderm, including the pharynx, vulva muscles, gonad distal
CC tip cells, intestine and several tail neurons. Isoform 2 is mainly
CC expressed in the organs derived from the ectoderm, including hypodermal
CC cells, head ganglion neurons and tail neurons (at protein level).
CC {ECO:0000269|PubMed:18632986, ECO:0000269|PubMed:20497576}.
CC -!- DEVELOPMENTAL STAGE: Isoform 1 is expressed in a cluster of cells in
CC the anterior half at 2.5 hours post fertilization (hpf), in hypodermal
CC cells at 5 hpf, in pharyngeal cells, intestinal and some neurons at 6
CC hpf. Isoform 1 is expressed in pharyngeal cells at L1 larval stage.
CC Isoform 1 is expressed in somatic gonad precursor cells (SGPs) during
CC the L2 larval stage. Isoform 2 is expressed in anterior neuronal cells
CC and posterior hypodermal cells at 5 hpf, in neurons of the head at 7.6
CC hpf (at protein level). Expressed in somatic gonad founder cells Z1 and
CC Z4, pharynx and muscles. {ECO:0000269|PubMed:15936327,
CC ECO:0000269|PubMed:18632986, ECO:0000269|PubMed:20497576}.
CC -!- PTM: Probably proteolytically processed to generate a N-terminal
CC intracellular domain. {ECO:0000269|PubMed:15936327}.
CC -!- DISRUPTION PHENOTYPE: Shows gonad disorganization, nerve cord
CC defasciculation and defects in distal tip cell migration and axonal
CC pathfinding. Shows local basement membrane deficiency and early gonad
CC disruption. {ECO:0000269|PubMed:18632986}.
CC -!- SIMILARITY: Belongs to the tenascin family. Teneurin subfamily.
CC {ECO:0000305}.
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DR EMBL; AB206835; BAD91086.1; -; mRNA.
DR EMBL; AB206836; BAD91087.1; -; mRNA.
DR EMBL; FO081247; CCD70175.2; -; Genomic_DNA.
DR EMBL; FO081247; CCD70183.1; -; Genomic_DNA.
DR EMBL; FO081246; CCD70183.1; JOINED; Genomic_DNA.
DR RefSeq; NP_001022723.2; NM_001027552.3. [G5EGQ6-1]
DR RefSeq; NP_741203.2; NM_171175.2.
DR AlphaFoldDB; G5EGQ6; -.
DR SMR; G5EGQ6; -.
DR BioGRID; 41168; 1.
DR STRING; 6239.R13F6.4e; -.
DR EPD; G5EGQ6; -.
DR PaxDb; G5EGQ6; -.
DR PeptideAtlas; G5EGQ6; -.
DR PRIDE; G5EGQ6; -.
DR EnsemblMetazoa; R13F6.4a.1; R13F6.4a.1; WBGene00006498. [G5EGQ6-2]
DR EnsemblMetazoa; R13F6.4a.2; R13F6.4a.2; WBGene00006498. [G5EGQ6-2]
DR EnsemblMetazoa; R13F6.4d.1; R13F6.4d.1; WBGene00006498. [G5EGQ6-1]
DR GeneID; 175953; -.
DR UCSC; R13F6.4a; c. elegans.
DR CTD; 175953; -.
DR WormBase; R13F6.4a; CE46838; WBGene00006498; ten-1. [G5EGQ6-2]
DR WormBase; R13F6.4d; CE42908; WBGene00006498; ten-1. [G5EGQ6-1]
DR eggNOG; KOG1225; Eukaryota.
DR eggNOG; KOG4659; Eukaryota.
DR InParanoid; G5EGQ6; -.
DR OrthoDB; 7516at2759; -.
DR PhylomeDB; G5EGQ6; -.
DR PRO; PR:G5EGQ6; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00006498; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR ExpressionAtlas; G5EGQ6; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0007411; P:axon guidance; IMP:UniProtKB.
DR GO; GO:0007413; P:axonal fasciculation; IMP:UniProtKB.
DR GO; GO:2001197; P:basement membrane assembly involved in embryonic body morphogenesis; IMP:UniProtKB.
DR GO; GO:0071711; P:basement membrane organization; IMP:WormBase.
DR GO; GO:0016477; P:cell migration; IMP:UniProtKB.
DR GO; GO:0030421; P:defecation; IMP:WormBase.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0010172; P:embryonic body morphogenesis; IGI:WormBase.
DR GO; GO:0008585; P:female gonad development; IMP:UniProtKB.
DR GO; GO:0007276; P:gamete generation; IMP:WormBase.
DR GO; GO:0008406; P:gonad development; IMP:WormBase.
DR GO; GO:0040039; P:inductive cell migration; IMP:WormBase.
DR GO; GO:0008584; P:male gonad development; IMP:UniProtKB.
DR GO; GO:0008045; P:motor neuron axon guidance; IMP:UniProtKB.
DR GO; GO:0060465; P:pharynx development; IMP:UniProtKB.
DR GO; GO:0048563; P:post-embryonic animal organ morphogenesis; IGI:WormBase.
DR GO; GO:0040032; P:post-embryonic body morphogenesis; IMP:WormBase.
DR GO; GO:0019953; P:sexual reproduction; IMP:WormBase.
DR CDD; cd00055; EGF_Lam; 1.
DR Gene3D; 2.120.10.30; -; 2.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR002049; LE_dom.
DR InterPro; IPR001258; NHL_repeat.
DR InterPro; IPR028916; Tox-GHH_dom.
DR Pfam; PF15636; Tox-GHH; 1.
DR SMART; SM00181; EGF; 7.
DR PROSITE; PS00022; EGF_1; 7.
DR PROSITE; PS01186; EGF_2; 7.
DR PROSITE; PS50026; EGF_3; 4.
DR PROSITE; PS51125; NHL; 4.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Developmental protein; Disulfide bond;
KW EGF-like domain; Membrane; Nucleus; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..2684
FT /note="Teneurin-1"
FT /id="PRO_0000421019"
FT TOPO_DOM 1..216
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 238..2684
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 463..499
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 501..534
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 650..684
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 716..753
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 1276..1317
FT /note="NHL 1"
FT REPEAT 1334..1378
FT /note="NHL 2"
FT REPEAT 1398..1441
FT /note="NHL 3"
FT REPEAT 1470..1513
FT /note="NHL 4"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 127..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 170..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 576..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 588..614
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 467..476
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 472..487
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 489..498
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 505..516
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 510..522
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 524..533
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 654..666
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 659..672
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 674..683
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 720..730
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 724..741
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 743..752
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT VAR_SEQ 1..182
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15936327"
FT /id="VSP_045023"
SQ SEQUENCE 2684 AA; 296470 MW; F7FBDFBA51AB2776 CRC64;
MFQHRTTNAQ GPPPNRPMPR PPAGMPMMTS SHEHDYTNDY EDPEEMARSR GEGFSNHLLI
KTTPPPQPHP NFNSYEMSMS QQRRSQQHQQ PMAPPLSDCW GSGVHDSGVL HKNADGAYYI
PSGSLRTTSS TLSPASGQRY LDQPHTSGGA PNPTYSDAST TLLKYPLAAG TNQNRRRQQV
GTMNNGDPVA GGPMALSKKK KKFDDDSDTC SRWPSKWNIL LAAALLVALF VICILLFRAP
NYVYTQPAPS SDATSSAAAA ASRYQDLGLR ALPPAISLGE RVDVEFFPKS MATTELTVTK
PSRIRFNATV GSGAQLVLLM SAGVHPSLSL HDALFPIRAD RIRDSKSPTH IVEEFGSRSR
RSLGASSSRH RNIEILSPRS ATFEQFVLEG RHYLTFINER SRVEPISFVA EELQRPTTPP
KTSSSGTSGA KEHPLASVLV CESNCNQRGE CVHGKCHCAP GFTGRTCDEA VCPVVCSGNG
VFSGGICVCK SGFKGKECEM RHNWCEVADC NGRGRCDTDG RCRCNPGWTG EACELRACPH
ASCHDRGVCV NGTCYCMDGW RGNDCSVFAD AIVHVPQAQS PPRRGQEPTE SSKTRKAQVK
PTPTSEKKKE SRELQKPIIA TVQVPTESSH PCSAHGQLID DICQCESGWD SVDCSQQACQ
CVNGDCLDDG SCQCWKGWRG SNCTDKKCAI GCEDRGKCAS DGSCKCSSGW NGENCAIDGC
PNQCSGKGEC GMDRRSSEWS CRCQAGSTGV DCSVSVEMHC DDGLDNDSDG LIDCDDPECC
SSSSCSSESV CSTAASPIEV LMRMPPIFNA NFAQRVGFLI MEKSVQSYTD SSQFNENLIS
VIRGRVMWGG SPTGSDDLST YSNKSTVPLV GVRVSDAAHP LYGFTLTRED GYFDLTVNGA
RSVTLQFLRT QFQSVKKSVF VSPRQIIHID DIVLYRQSGG SPPAISMAPA RAKCSPTLRR
IPDVVLISNW QYTSDGIETD ETSDSSRIVV DSRSIFESLP IQGTDVRLVY DSARSPAAPS
TMLIGLLYDR VDKELRKVHI NIRIAGRRFD RVLAPRTNLT YVFAWDKMNA YRQSESGLVP
VTVRVGYEYQ GCDRTSERVW QTRRSQMMGA TARKMIGTMW TLDIHHHLDI VNNVVEMGNG
GYRLITESEP RVSTFAGLDG VKRDVECLKC EGKVDSISLF RPTTVVYAQD GSLIIGDHNM
IRRVSQDGQV STILTLGLAD TSHSYYIAVS PVDGTIAISL PLHKQVWRIS SLEPQDSRNN
YDVLAGDGTV CASAVDSCGD GALAQNAQLI FPKGISFDKM GNLYLADSRR IRVIDTTGHI
RSIGETTPDQ HPIRTCAQIT KLVDLQMEWP TSLTIDPITG SVLVLDTNVV YEIDVVHDVV
TIALGSPTTC DLANATSSAS AKSLDHRRHL IQNARDITVG TDGAIYVVES DGRRLNQVRK
LSSDRSTFSI LTGGKSPCSC DVAACGCDDA VSLRDVAASQ AHLSSPYAVC VSPSGDVIIA
DSGNSKIKKV SARMAKYDGR SRTYEVTDAE RQEKYTFNRH GQHSSTVSLI TGRTFFNFSY
QVDSPISMIS EIRAASGVVL RVLKRNDSLF DLETTLGQRT TLTMSAYDGT LEQVSKRDSA
TSRDATKLFY KKGLLTSRID VATAVGFEYD EYGRAIGLKR DREYWRLGEE TISMGSVNTE
VLLNGQRFQQ VRLGEGNLAV HSTNGATTRL ISLRNEGYSL ASPLGTSTLY DKSSSIPDSN
GEPLISRRRT KVPAIGNPQR RELTTRWDWR HVARRGDDSD GSLGRRKVAE INGVNMFSME
YDVKSNQDTL RLGSTTDDAQ ALLFIDYTSS GRIRRISAPE DSQMAEMNIT WDGAGRKSEV
TWGSWKIRLT YDNSNRLTEH AIDGARVPIK MSYAGASRRP NEIQHDGAKW NIQYDNYDRI
KEVISKSQEA TSFSSIALGG DEWVLKRRTS LNSKPSLVRL SREGKVLEST TPDENHYWLE
RKDPITGRTT EILNDEETTV VTCWSPEGAP MCSRSRNLQE NTTMQGHLVA RKSVTIMTPT
SSEPSITSSF TYEYDDMLRV TTIQPVIEQS VLESIQLSYD ERRGHVAAIN GFKWARDAST
SRCQGHGLMY ETSKANDHRQ VVERKLIFGD ARASIKIIRD KAGRASESHL EISSSGTQRN
QKITRTFDAA GRVASVEQND QEPVRIIWNS DARVEKINDR VVEWNRGGAL KTFQDISYQV
DSIGWVVKRD NTTVFGYDGK GRLVSARSSQ LRINIFYDRE DRVVQIQNSK DFIHFYYGYI
DTPKLVSHFS KNGKISTLFY DDDSVPFAMQ SDDGTRYALL TDETSTIKAI IGDSNVLRII
DRSVFGALLP SSSSSHPFLP IGYLGGIEIS EISVSILNNG RPLDLYSERY MSISPEAVVR
LELNEKFSNS IDLMALEIDR QPFRVENVPE DFETWFSLAG LSPNLLPSAH LGLPASSAIV
HRLLSSFPRK LRPLTHLTTV LPTRLASDIS LTSPTSETSW SIDDVGFSNL LILNEDATTG
EVMVEMLSDL KSEEREVISK LFDGVKSLDF ATWGLVPTRH LWRAPNSKLE LSSTSFSHFT
MAVNKDSVEL RNGKSKIVVH FSENKAEIVK KIVEELKTRE NIAVWRAERK RAEAGEKTWR
QWSDRETREL TSKGSVSGYD IEMKPAHQSG LLASVHSWKF RKSE
