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Database: UniProt
Entry: W5KIH5_ASTMX
LinkDB: W5KIH5_ASTMX
Original site: W5KIH5_ASTMX 
ID   W5KIH5_ASTMX            Unreviewed;      2718 AA.
AC   W5KIH5;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 2.
DT   27-MAR-2024, entry version 60.
DE   SubName: Full=Teneurin-1-like {ECO:0000313|Ensembl:ENSAMXP00000007387.2};
GN   Name=TENM1 {ECO:0000313|Ensembl:ENSAMXP00000007387.2};
OS   Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC   Characoidei; Characidae; Astyanax.
OX   NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000007387.2, ECO:0000313|Proteomes:UP000018467};
RN   [1] {ECO:0000313|Proteomes:UP000018467}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA   Jeffery W., Warren W., Wilson R.K.;
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000018467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX   PubMed=25329095; DOI=10.1038/ncomms6307;
RA   McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA   Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA   Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA   Yoshizawa M., Warren W.C.;
RT   "The cavefish genome reveals candidate genes for eye loss.";
RL   Nat. Commun. 5:5307-5307(2014).
RN   [3] {ECO:0000313|Ensembl:ENSAMXP00000007387.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC       pass membrane protein {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; 7994.ENSAMXP00000007387; -.
DR   Ensembl; ENSAMXT00000007387.2; ENSAMXP00000007387.2; ENSAMXG00000007150.2.
DR   eggNOG; KOG4659; Eukaryota.
DR   GeneTree; ENSGT01030000234566; -.
DR   HOGENOM; CLU_000229_0_0_1; -.
DR   InParanoid; W5KIH5; -.
DR   OrthoDB; 5491728at2759; -.
DR   Proteomes; UP000018467; Unassembled WGS sequence.
DR   Bgee; ENSAMXG00000007150; Expressed in brain and 1 other cell type or tissue.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
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; 6.
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; IPR011044; Quino_amine_DH_bsu.
DR   InterPro; IPR022385; Rhs_assc_core.
DR   InterPro; IPR009471; Ten_N.
DR   InterPro; IPR028916; Tox-GHH_dom.
DR   NCBIfam; TIGR03696; Rhs_assc_core; 1.
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; 2.
DR   Pfam; PF15636; Tox-GHH; 1.
DR   SMART; SM00181; EGF; 8.
DR   SUPFAM; SSF49464; Carboxypeptidase regulatory domain-like; 1.
DR   SUPFAM; SSF57196; EGF/Laminin; 1.
DR   SUPFAM; SSF101898; NHL repeat; 1.
DR   SUPFAM; SSF50969; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR   PROSITE; PS00022; EGF_1; 5.
DR   PROSITE; PS01186; EGF_2; 4.
DR   PROSITE; PS50026; EGF_3; 4.
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   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018467};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        299..322
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          110..297
FT                   /note="Teneurin N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51361"
FT   DOMAIN          567..599
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          633..666
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          697..728
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          737..772
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          87..189
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          203..226
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          353..374
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        26..52
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        128..148
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        169..186
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        589..598
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        656..665
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        701..711
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        718..727
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        741..751
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        762..771
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   2718 AA;  300258 MW;  354E127511CD5A19 CRC64;
     MDDNVYQSLS RPRPGMELSY SSSSEEDEGA DLRHKHYRDT HSHTHSDYEP DRRFTYNSHK
     VRRKPNELTQ KEPAQMAFPD FQTELHSANQ ELAYPGGGAS VGMASDPESE GGASPDHALR
     LWMQEVKSER TSCVSSRANS VLSLTDTEQE GRGEQDNDND LPSSPVARFS FRPLPPPPPP
     PHACTCVRPA PSAAPELIQR NTLPARGHQS ESSKTAQDDS GQSENTWALN SNIPLETRHF
     LFKHGSGSST LFNATNQNYP LTSSTVYSPP PRPLPRAPLS RPLFSFSKPY RCCNWKCTAL
     SASAVTVTLA LLLTYVIVVN LLGLPWSLRR LDAELFENGK AGRSQEEGND LISTAQLPTP
     NTSHTDKDPL QRGRGIDRGE VDIGMQMVQV IPPGQFWRFS VVVQHPEYVR FNITHTHNAL
     LGIYGRRNLP PTHTQFDFVK LLDGKLKQES RISDFTKVSS GLLTALQETV FMEYLDLGNW
     HLAFYNDGRK MEQVQVHSTA VEMMDGCSTN CNGNGECVAG HCHCFTGFLG PDCSKDSCPV
     LCSGNGEYEK GVCACRVGWK GAECEVEDGQ CIDPTCSNNG ECVDGTCVCA PAFKGNNCEE
     VDCVDPTCSG RGVCVRGECV CSAGWGGEVC ETPLPACKEQ CSRHGTYNPE TGVCVCEQGW
     TGTDCSTEVC PLPCSVHSVC AGGRCQCEDG WEGPTCDRQA CHPSCEEHGE CRDGQCVCHP
     GWEGEHCTIA HYLDLLDKDA CPGLCNGNGR CTLEQSGWHC VCQSGWSGPG CNIVMETQCN
     DSGDNDGDGL VDCVDPDCCS QQVCANSPLC QGSPDPRDII QQNHAPFGPR PSLQFFDRVQ
     FLVRRGSTHI LPGDLPYDSS RVCVIRGQVV SSDGTPLVGV NVTFQQNPEY GYTLSRQDGS
     FDLLAVGGVS ITLLFQRAPF LPLTRSLWLP WNQFVVLGSV MMSRSEPRPP VCEDKNLIGP
     NPTVLPAPLT LFAGNCQERG PVIPELQAVQ EEIEIAGSFL KLSYLSTRSP GYRSLLRVIL
     THSLLPVGLA KVHLSVSVEG TLVTKWFPAS PNLIYVFSWN KTDVYGQQVT GLVQALVSVG
     YEYESCPDFI IWQKRTAQLQ GFELISSHLG GWALDKHHTL NLESGILHKG DGENVFISQQ
     PPLISTVMGT GTVRPIACPS CNGPAAERKL FAPVALACGS DGSIYVGDFN FIRRILPNGF
     TVSILELRNR DIRHSTSPAH KYYLALDPVS EALYVSDSSS RRVLRLKAVT EPRDLSRNAE
     VLAGNGEQCT PFHPNQCGDG GKATEASLIS PRGIAVDKYG SVYFVDGTTV RKIDKGIITT
     VMGSNGLTST QPISCDTHMD ISQVRLEWPT DLAISPLDNS LYVLDNNLVL QVSEAGLVRV
     VAGRPIHCPL AITDPTTLGP ASTRLMLEGA KAIAVSHQGV LYIAQTDDRK LSRVLEVNSN
     GEMSTVAGTA SECDCKIDPD CDCFSGDGGY ARDAKLKSPS ALAVSPNGTL YIADLGNVRV
     RSLVARRPRL TSDLLYEVMS VAQQEVYLFS PNGSHLYTRC LVTGDYLYNF TYVGAGLISA
     VTASEGGAVQ VRRDSNGAPL WLVTPGGQVY WLNLSSAGTL RRVSALAHDL AQISYHGNTG
     LLATMSNENA WTTVYEYNSD GHLINVTLPT GEVSSLHGDM GKSVKVEALT SNRENFITIT
     NHSEDNTIYT LRQAHSVSVY RVSGDGSLWV TYASGMDVTL STEPHLLPGA LPGVTPGVVH
     PTVGRCNITL PGEQIHSIIE WRQRREQARN YSTYERRLRA HNRNVLSIDY NQASRVGKVY
     DDHRKFTLRL QYDDRGRPVL WAPSKFSDVR VSYTNDGLLA SIQRGNWSER RDYDNSRLIS
     RTWANGKTWS YSFQEKSVQL LLHSQRRYTF EYDQTDYLMS ITLPSMVKHG LQTALSIGYY
     RNTYTPPDAP GHALVQDYTP DGRLLQTLYM GSGRRVLYKY SRTSRLSEIL YDSTLVSFTY
     DESSGAIKTV HLMQEGFVCT IRYRQTGPLV GRQIYRFSEE GLVNARFDYS YNNFRVTSMQ
     AMINETPLPI DLYRYVDVSG RVEQFGKFSV ISYDLNQVIT THAMKHTKIF NPNGQVVEVQ
     YEILKSIAFW MTLQYDNLGR IGNCDIRIGV DGNITRRSYE YDADGQLQSV AVDDRPQWRY
     SYDLNGNINL LSHGNSARLT PLRYDLRDRI TRLGEIQYKT DDDGFLRVRG NVVFDYTSNG
     LLAGALDRDS GKRVWYRYDG LGRRVSTRTS DGALLQFFYA DLNEPTRVTH WYNHTASEIT
     SLYYDLQGHL IAMEMSSGQE FYIACDAAGS PLAIFSSRGQ VVKELRYTPY GDVYRDSNPS
     FQLPFGFQGG LYDPLTRLVH LGRRDYDVVA GRWTTPNHDL WAEVSADPKP FNLYAFKNNY
     PLGALQDVTK FTTDISSWLQ LFGFQLHNVV PGFPKLPVEN TEQTYEMMNV QSRTHSWDPS
     KVVLGIQCEL QKLLQNFISL DRLPMTPAKS KPGGLRGRSP RFSALSSIFG KGVKFAVCAD
     GVISAEIIGV ASEDSRRIAA VMNGAVYLRG VRFTVDGRDT HYFTKDSPLE ADLGVVWGGS
     GAAGGGARVL ENGVNVSVSQ MSAVVAGETR RFADLVLQQG ALCFNIRYGA TPDEERTRVL
     EGARLRAVTG AWLLEQRRVR DGEGGARVWT NKEKDELLSD GHVSGYEGFY VLPVEQHPEL
     ADSPFNIQLI RQTDAGRR
//
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