ID I3IXW7_ORENI Unreviewed; 2758 AA.
AC I3IXW7;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 76.
DE SubName: Full=Teneurin transmembrane protein 3 {ECO:0000313|Ensembl:ENSONIP00000001457.2};
GN Name=TENM3 {ECO:0000313|Ensembl:ENSONIP00000001457.2};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000001457.2, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Proteomes:UP000005207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Broad Institute Genome Assembly Team;
RG Broad Institute Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSONIP00000001457.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004162};
CC Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004162}. Membrane
CC {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004167}.
CC -!- SIMILARITY: Belongs to the tenascin family. Teneurin subfamily.
CC {ECO:0000256|ARBA:ARBA00009385}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR STRING; 8128.ENSONIP00000001457; -.
DR Ensembl; ENSONIT00000001456.2; ENSONIP00000001457.2; ENSONIG00000001151.2.
DR eggNOG; KOG4659; Eukaryota.
DR GeneTree; ENSGT01030000234566; -.
DR HOGENOM; CLU_000229_0_0_1; -.
DR InParanoid; I3IXW7; -.
DR OMA; GRESEHT; -.
DR TreeFam; TF316833; -.
DR Proteomes; UP000005207; Linkage group LG2.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd00053; EGF; 1.
DR CDD; cd00055; EGF_Lam; 1.
DR Gene3D; 2.10.25.10; Laminin; 5.
DR Gene3D; 2.180.10.10; RHS repeat-associated core; 1.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 2.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR008969; CarboxyPept-like_regulatory.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR002049; LE_dom.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR022385; Rhs_assc_core.
DR InterPro; IPR031325; RHS_repeat.
DR InterPro; IPR009471; Ten_N.
DR InterPro; IPR028916; Tox-GHH_dom.
DR InterPro; IPR006530; YD.
DR NCBIfam; TIGR03696; Rhs_assc_core; 1.
DR NCBIfam; TIGR01643; YD_repeat_2x; 1.
DR PANTHER; PTHR11219; TENEURIN AND N-ACETYLGLUCOSAMINE-1-PHOSPHODIESTER ALPHA-N-ACETYLGLUCOSAMINIDASE; 1.
DR PANTHER; PTHR11219:SF63; TENEURIN-3 ISOFORM X1; 1.
DR Pfam; PF05593; RHS_repeat; 1.
DR Pfam; PF06484; Ten_N; 1.
DR Pfam; PF15636; Tox-GHH; 1.
DR SMART; SM00181; EGF; 8.
DR SUPFAM; SSF49464; Carboxypeptidase regulatory domain-like; 1.
DR SUPFAM; SSF101898; NHL repeat; 1.
DR SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1.
DR PROSITE; PS00022; EGF_1; 3.
DR PROSITE; PS01186; EGF_2; 3.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS51361; TENEURIN_N; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000005207};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 361..386
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 22..361
FT /note="Teneurin N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51361"
FT DOMAIN 791..826
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 226..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..248
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..269
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 795..805
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 816..825
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 2758 AA; 305725 MW; B593A8F9A0EC2422 CRC64;
LQDENQSHRR KRRGGKKDKD RERRYTASSS DRDEGACRVP TQKSYSSSET LQAFDHDPSR
MLFGGRVKEM VHKETAEYTR PGQTFSLRQL GICEPPARRG LALCPETGLS HPLSSYSRGP
VATENHEPVS PERTITLWGT GAKSGQNSCL SSRSNSALTL TDTEMDNKSD NEMGDYSLLS
DLLTCHKCTV PPTNRKEKIM CTFPREKSHG YLNSYADACF SLASSPGDHL SSQQAPPPLP
PAPPPHKQHP SITSLSRSSL ANQRSPSPPP TAGLAADLQS TAECVQLQDS WVLGSNVALE
SRHFLFKTGT GTTPFFGAAA PGYTMATGTV YSTPARPLPR NSLSRGAFKF KKSPKHCSWK
CTALIAVGIA VVLSIILCYC IAMHLFGLNW QLQELDNQPA FENGGVGKTG PTQSSVGTAL
AADGRTSVLH PENNSIDTGQ VDIGKRVGQS IPPGVFWRSQ INMEEPGFLK FNISVQKNAL
IGVYGRKGLA PSHTQYDFVE LLDGSRLIAK EHRALSEPDT RARSDPVAVH QAGFIQYLDS
GVWHFAFYND GRNVETVSYN TIIQESVTEC THKCYGNGEC VAGSCHCFPG FIGPYCSRAA
CPVLCSGNGQ YTRGRCQCYS GWKGTECDVP ASQCIDPQCG GHGLCVAGNC ACNTGHKGTN
CEQVDCADPT CSGHGACHHG ECHCNPGWGG ISCEILKSTC PEQCSSHGTF NTDSGTCICE
ANWTGADCSI EVCVVDCGPH GSCISGVCHC EEGWTGPECE QRDCHPRCID HGVCREGKCD
CHQGWTGEHC TIDGCPGLCN NNGRCVLDQN VWHCICQSGW RGLGCDVATE TLCSDGKDNE
GDGLIDCMDP DCCTQIACQG QTYCRGSPDP AAIASQSQSS AAQSSSKSFY ERVSFLIGPS
GSHVIPRDNP FNSSLASVIR GQVLTGDGTP LIGVNVSFLH YPEYGYTITR QDGMFDLLAN
GGASLTLSYE RAPFPTLHRT VWLPWNVFHV MDTVVMKREE NDIPSCYLTG LVRPNPVILA
TPLSTLYKTS PEDSPIIPET QVLHEQVAIP GSDLNLVYLS SRAAGYKPIL KVLLTQDRLP
FGLMKVHLMV AVMGRQFQKS FPAFPDLSYT FIWDKTDAYN QKVFGLAEAV VSVGYEYESC
LDVVLWEKRT AVLQGYELDA SNMGGWMLDK HHILDIQNGI LYKGSGENQF ISLQPPVIST
VMGNGRRRSI SCPSCNGQAQ GNKLLAPVAL AWGIDGSLYV GDFNYIRRIY PSGNVTSIME
LRNKDFRHSN NPAHRYYLAT DPVSGQLYVS DTNSRRIYRP RTLAGSKDLP SNAEVVAGTG
EHCLAFDEDH CGDGGKAPEA SLTGPKGIAV DKNGLIYFVD GTTIRKVDQN GIISTFLGSN
DLTSARPLTC DNSMDINQVN LEWATDLAVS PMDNSLYVLD NNIVLRISEN GQVSIAAGRP
THCPLAGLER GVAGGQRAQL TPLESAVSIA ISYHGAIYIA ETDERKMSRI RKVSVDGEIT
HLAGAPSDCD CKNDANCDCY QTGDGYAKDA RLNAPSSLVA APDGTLYVAD LGNIRIRAIS
RNGPTSSANT YEVASPDAQE LYVFDSNGTH QHTASLLTGD LKYTFSYSTE NDITAVTDSS
GNTLRIRRDP NRMPVRIVAP DNQVIWMTMS TNGGLKTLTA QGQELVLLTY HGNNGLLATK
TSEIGWTTFY DYDSEGRLMN VTFPTGMVNN LYTDLYSALT VDIESSMTEE EISITTNTST
VRAFYTLAQD QCRSSYQVGY DNSLRITYAN GMDTHYQTEP HILAGAANPT VARRNMSLPG
ESGQNLVEWR FRKEQARGKV IVFGRKLRVN GRNILSVDYD RTLRTEKIYD DHRKFLLKII
YDTAGHPVLW VPSSKLLPVN VSRTSSGQIS ALQRGPTTER LEYDSQGRLI SRVFADGKIW
SYTYLEQSMV LLLHSQRQYI FDFDSLDRLS AVTMPSVARY TMQTIRSVGY YRNLYHPPES
NASVAVDYSE DGLLLRIAHF GTGRRVLYRY RRQNKLSEIL YDSTRVSFTY DETAGVLKTV
NLQNEGFICS IRYRQVGPLV DRQIFRFSED GMVNARFDYT YDSSLRVTSV QGVINETPLP
IDLYQFDDIS GKVEQFGKFG VIYYDINQII STAVMTYTKH FDAHGRIKEI QYEIFRSLMY
WITFQYDDVG RVTKREIKIG PFANTTKYSY EYDVDGQLQT VFLNDKVMWR YTYDLNGNLH
LLNAGNSARL LPLRYDLRDR ITRLGDIQYR MDEDGFLRQR GAEIFEYNSK GLLVRVYSKS
SGWTIQYRYD GLGRRVSTKS SLGQHLQYFY ADLSYPARIT HVYNHSSSEI TSLYYDLQGH
VFAMEISSGE EFYIACDNTG TPLAVFTSNG LLVKQLLYTA YGEVYLDSNP DFQLVLGFHG
GLYDPLTKLL HFGEKDYDIM SGRWTIPDVS AWKKIGKEPV PFNLYMFRNN NPISKVHEVK
EYVADVNTWL VTFGFHLHNT IPGFPVPKFD LSMPSYELRK SQLWDDLPSI SGVQQEVTRQ
AHSLLSFERL PEVHLNRGRR GEKSWLWFSA AMSPIGRAVM FAIYKGSVHT HTLNVASEDC
IKVASILNNA FYLEDLHFTI EGRDTHYFVK PGLPDADLAA LHLTSGHKTL ENGVNVTVSQ
STTVMDSRTR RFADVEIRAG ALAFHIRYGS TVDEEKARVI ELARQRALAG AWAKEQQRVR
DGEEGVRPWT EGEKRQLLSS GKVLGYDGYY VLSIEQYPEL ADSTNNIHFL RQSEIGKR
//
