ID S7N3W9_MYOBR Unreviewed; 2512 AA.
AC S7N3W9;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=Teneurin-1 {ECO:0000313|EMBL:EPQ11744.1};
GN ORFNames=D623_10033177 {ECO:0000313|EMBL:EPQ11744.1};
OS Myotis brandtii (Brandt's bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=109478 {ECO:0000313|EMBL:EPQ11744.1, ECO:0000313|Proteomes:UP000052978};
RN [1] {ECO:0000313|Proteomes:UP000052978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23962925; DOI=10.1038/ncomms3212;
RA Seim I., Fang X., Xiong Z., Lobanov A.V., Huang Z., Ma S., Feng Y.,
RA Turanov A.A., Zhu Y., Lenz T.L., Gerashchenko M.V., Fan D., Hee Yim S.,
RA Yao X., Jordan D., Xiong Y., Ma Y., Lyapunov A.N., Chen G., Kulakova O.I.,
RA Sun Y., Lee S.G., Bronson R.T., Moskalev A.A., Sunyaev S.R., Zhang G.,
RA Krogh A., Wang J., Gladyshev V.N.;
RT "Genome analysis reveals insights into physiology and longevity of the
RT Brandt's bat Myotis brandtii.";
RL Nat. Commun. 4:2212-2212(2013).
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 EMBL; KE163382; EPQ11744.1; -; Genomic_DNA.
DR eggNOG; KOG4659; Eukaryota.
DR Proteomes; UP000052978; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd00054; EGF_CA; 2.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 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; IPR009471; Ten_N.
DR InterPro; IPR028916; Tox-GHH_dom.
DR InterPro; IPR006530; YD.
DR NCBIfam; TIGR01643; YD_repeat_2x; 3.
DR PANTHER; PTHR11219; TENEURIN AND N-ACETYLGLUCOSAMINE-1-PHOSPHODIESTER ALPHA-N-ACETYLGLUCOSAMINIDASE; 1.
DR PANTHER; PTHR11219:SF7; TENEURIN-1; 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; SSF82171; DPP6 N-terminal domain-like; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF101898; NHL repeat; 1.
DR PROSITE; PS00022; EGF_1; 5.
DR PROSITE; PS01186; EGF_2; 4.
DR PROSITE; PS50026; EGF_3; 3.
DR PROSITE; PS51361; TENEURIN_N; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
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:UP000052978};
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 98..123
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..98
FT /note="Teneurin N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51361"
FT DOMAIN 372..404
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 502..533
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 541..576
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 394..403
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 506..516
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 523..532
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 545..555
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 566..575
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 2512 AA; 281022 MW; AB586FEDFB8FE3D6 CRC64;
MTTRSQPSPA APAPPTSTQD SVHLHNTWVL NSNIPLETRH FLFKHGSGSS AIFSATSQNY
PLTSNTVYSP PPRPLPRSTF SRPAFTFNKP YRCCNWKCTA LSATAITVTL ALLLAYVIAV
HLFGLTWQLQ PVEGQLYENG VSKGNRGTES MDTTYSPIGG KVSDKSEKKV FQKGRAIDTG
EVDIGAQVMQ TIPPGLFWRF QITIHHPIYL KFNISLAKDS LLGIYGRRNI PPTHTQFDFV
KLMDGKQLVK QDSKGSDDSQ HSPRNLILTS LQETGFIEYM DQGPWYLAFY NDGKKMEQVF
VLTTAIEIMD DCSTNCNGNG ECISGHCHCF PGFLGPDCAR DSCPVLCGGN GEYEKGHCVC
RNGWKGPECD VPEEQCIDPT CFGHGTCIMG VCICVPGYKG EICEEEDCLD PMCSSHGICV
KGECHCSTGW GGISCETPLP ICQEQCSGHG TFILDTGMCS CDPKWTGSDC STELCTMECG
SHGVCSRGIC QCEEGWVGPT CEERSCHSHC AEHGQCKDGK CECSPGWEGD HCTIAHYLDA
VRDGCPGLCF GNGRCTLDQN GWHCVCQVGW SGTGCNVVME MLCGDNLDND GDGLTDCVDP
DCCQQSNCYI SPLCQGSPDP LDLIQQSQPL FSQHTSRLFY DRIKFLIGKD STHVIPPEIS
FDSRRACVIR GQVVAVDGTP LVGVNVSFLH HSDYGFTISR QDGSFDLVAI GGISVTLIFD
RSPFLSEKRT LWLPWNQFIV VDKVTMRRVV SDPPSCDISN FVSPNPIVLP SPLTSFGGSC
PERGTIVPEL QVVQEEIPIP SSFVRLSYLS SRTPGYKTLL RILLTHSTIP MGMVKVHLTV
AVEGRLTHKW FPAAANLVYT FAWNKTDIYG QKVWGLAEAL VSVGYEYETC PDFTLWEKRT
VILQGFEMDA SNLGGWSLNK HHIFNPQSGI IHKGNGENMF ISQQPPVIST IMGNGHQRSV
ACTNCNGPAH NNKLFAPVAL ASGPDGSVYV GDFNFVRRIF PSGNSVGILE LRNRDTRHST
SPAHKYYLAM DPMSESLYLS DTNTRKVYKL KSLVETKDLT KNFEVVAGTG DQCLPFDQSH
CGDGGRASEA SLNSPRGITV DRHGFIYFVD GTMIRKIDEN AVISTVIGSN GLTSTQPLSC
DSGMDITQVR LEWPTDLAVN PMDNSLYVLD NNIVLQISEN RRVRIIAGRP IHCQVPGIDH
FLVSKVAIHS TLESARAISV SHSGLLFIAE TDERKVNRIQ QVTTNGEISI MAGAPTDCDC
KIDPNCDCFS GDGGYAKDAK MKAPSSLAVS PDGTLYVADL GNVRIRTISR NQAHLNDMNL
YEIASPADQE LYQFTVNGTH LHTLNLITRD YVYNFTYNAE GDLGAITSSN GNSVHIRRDA
GGMPLWLVVP GGQVYWLTIS SNGVLKRVSA QGYNLALMTY PGNTGLLATK SNENGWTTVY
EYDLEGHLTN ATFPTGEVSS FHSDLEKLTK VELDTSNHEN VLMSTNLTAT TTIYILKQEN
TQSTYRVNPD GSLRVTFASG MEISLSSEPH ILAGAVNPTL GKCNISLPGE HNANLIEWRQ
RKEQNKGNVS AFERRLRAHN RNLLSIDFDH ITRTGKIYDD HRKFTLRILY DQTGRPVLWS
PVSRYNEVNI TYSPSGLVTF IQRGMWNEKM EYDQSGKIIS RTWADGKIWS YTYLEKSVML
LLHSQRRYIF EYDQSDCLLS VTMPSMVRHS LQTMLSVSYY RNIYTPPDSS TSFIQDYSRD
GRLLQTLHVG TGRRVLYKYT KQARLSEILY DTTQVTLTYE ESSGVIKTIH LMHDGFICTI
RYRQTGPLIG RQIFRFSEEG LVNARFDYSY NNFRVTSMQA VINETPLPID LYRYVDVSGR
TEQFGKFSVI NYDLNQVITT TVMKHTKIFS ANGQVIEVQY EILKAIAYWM TIQYDNMGRM
VICDIRVGVD ANITRYFYEY DADGQLQTVS VNDKTQWRYS YDLNGNINLL SHGNSARLTP
LRYDLRDRIT RLGEIQYKMD EDGFLRQRGN DIFEYNSNGL LQKAYNKASG WSVQYYYDGL
GRRVASKSSL GQHLQFFYAD LANPIRVTHL YNHTSSEITS LYYDLQGHLI AMELSSGEEY
YVACDNTGTP LAVFSSRGQV IKEILYTPYG DIYHDTYPDF QVIIGFHGGL YDFLTKLVHL
GQRDYDVVAG RWTTPNHHIW KQLNLLPKPF NLYSFENNYP VGKIQDVAKY TTDIGSWLEL
FGFQLHNVLP GFPKPELENL ELTYELLQLQ TKTQEWDPGK TILGIQCELQ KQLRNFISLD
QLPMTPRYND GRCLEGGKQP RFASVPSVFG KGIKFAIKDG IVTADIIGVA NEDSRRLAAI
LNNAHYLENL HFTIDGRDTH YFIKLGSLEE DLVLIGNTGG RRILENGVNV TVSQMTSVLN
GRTRRFADIQ LQHGALCFNI RYGTTVEEEK NHVLEIARQR AVAQAWTKEQ RRLQEGEEGI
RAWTEGEKQQ LLSTGRVQGY DGYFVLSVEQ YLELSDSANN IHFMRQSEIG RR
//
