ID A0A1S3RDX9_SALSA Unreviewed; 2726 AA.
AC A0A1S3RDX9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Teneurin-3-like isoform X9 {ECO:0000313|RefSeq:XP_014050568.1};
GN Name=LOC106602442 {ECO:0000313|RefSeq:XP_014050568.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014050568.1};
RN [1] {ECO:0000313|RefSeq:XP_014050568.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014050568.1};
RG RefSeq;
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 RefSeq; XP_014050568.1; XM_014195093.1.
DR OrthoDB; 5491728at2759; -.
DR Proteomes; UP000087266; Chromosome ssa04.
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; 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; IPR022385; Rhs_assc_core.
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:SF65; TENEURIN-3; 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; SSF101898; NHL repeat; 1.
DR SUPFAM; SSF63825; YWTD domain; 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 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:UP000087266};
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 316..341
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..316
FT /note="Teneurin N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51361"
FT DOMAIN 616..648
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 650..683
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 754..789
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 144..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 638..647
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 673..682
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 758..768
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 779..788
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 2726 AA; 303984 MW; 8582F82DB07143B6 CRC64;
MDVKERRPYC SLTKSRRDKE RRYTGSSGDS EECGSGGPGP RVPTQKSYSS SETLKAFDHQ
DSSRLLYSSR VKEMVHREQD EYTRQGQNFN LRQLGICEPS TRRGLAFCAE MGLPHRGYSV
GAGSDVDPEN EGVMSPERAM RLWGRGVKSG GRNSCLSSRS NSALTLTDTE HENKSDSDNE
QPSNHHQQGQ STLPPAPPPH KQQPSVTALN HNSLSSRNRN PSPAPPAALP AELQTTPESV
PLQDSWVLGS NVPLESRHFL FKTGTGTTPL FSTATPGYTM ATGSVYSPPT RPLPRNTLSR
SAFKFKKSSK YCSWRCTALS AVGLSVLLSV LLCYCIAMHL FGLNWQLQET EGYTFENGLG
RSDTTPNTIT ALSADNGKLG VFLQENNTID TGEVDVGRRA VQEVPPGIFW RSQLYIDQPQ
FLKFNISVQR DALVGVYGRK GLPPSHTQYD FVELLDGSRL ITKEKRGLVE VEGVSRRARS
VSVHEAGFIQ YLDSGIWHMA FYNDGKNSEQ VSYNTIVIES VMECPHNCHG NGDCLSGTCH
CFPGFLGPDC SRASCPVLCS GNGQYSRGRC LCFSGWKGTE CDVPSNQCID IHCGGHGICI
IGVCVCNTRY KGDNCEEVDC LDPGCSAHGV CIHGECHCSP GWGGTNCEIL KTMCPDQCSG
HGTYQSESGT CTCDTNWTGP DCSIEVCVVD CGSNGVCFGG SCRCEEGWTG TVCDQKACHP
MCTKNGVCKE GKCECNQGWT GEHCNIAHNP DIRVKEGCPG LCNNNGRCTL DQNGWHCVCQ
SGWRGAGCDV AMETLCTDGK DNEGDGLADC MDPDCCLQTS CQTQPYCRGS PDPSEIISQS
PSSLMPQHAA RSFYQRIRFL VGPEGSHVIT GDNPFNKSLV SIIRGQVLTA DGTPLIGVNV
TFVHYPDHGY TITRKDGMFD LLTNGGASLT LSFERAPFLI QYHTVWIPWN VFYVIDTLVM
KKEENDIPSC DLSGFIRPSP VIVASPLSTC FRSSPEDGPI IPETQVLQEE TSIPGSDLNL
LYLSSRAAGY KPVLKVTMTQ ASVPFNLMKV HLMVAVVGRL FQKWFPAQPN LSYTFIWDKT
DAYNQKVYGL SEAVVSVGFE YESCLDLILW EKRTATLQGY ELDASNMGGW TLDKHHILDI
QNGILYKGNG ENVFISQQPP VISSIMGNGR RRSISCPSCN GQAEGNKLLA PVALACGADG
SLFVGDFNYI RRIFPSGNVT SVMELRNKDF RHSNNPAHRY YLATDPVTGQ LYVSDTNSRR
IYRPKVLTGT KELIQNGEVV AGTGEQCPPF DEARCGDGGK ATEALLMGPK GITVDKNGYI
YFVDGTMIRK VDRNGIISTL LGSNDLTSAR PLTCDTSMHI RQVRLEWPTA LAINPMDNSI
YVLDNNVVLQ ITENRQVRIV AGRPMHCQVP GIEYMLGKRA VQTMLEGAAA IALSYSGVLY
IAETDEKKIH RIRQVSTDGE ITPLAGALSD CDCKNDANCD CYQTGDGYAK DARLNSPSSL
VVSPDGTLYV ADLGNIRIRA VRRNQPPSGS AVSGPGSFEV ASPSSQELYV FDSNGTHQFT
MSLVTGDYKY NFSYSNEEDV TAVTDSSGNT LRIRRDPNRM PVRIVAPDNQ VIWLTIGTNG
GLKTLTAQGQ ELVLFTYHGN SGLLATKTIQ IGWTTFYDYD SEGRLTNVTF PTGVVTNLHG
DMTGAITVDI ETSGRDEDVS ITTNLSSIDS FYTLVQDQLR NSYQVGYDHS LRVIYANGMD
THYQTEPHIL AGAANPTVAR RNMTLPGENG QNLVEWRFRK EQTRGKVIVF GRKLRVNGRN
LLSVDYDRTL RTEKIYDDHR KFLLKIVYDT QGHPTLWVPS SKLLSVNLTY SSTGQVTSLQ
RGPTTERVEY DGQGRIVSRV FADGKTWSFT YLDKSMVLLL HSQRQYIFDY DLLDRLSAVT
MPSVARHTMQ TIRSLGYYRN IYNPPESNAS VTVDYSEDGQ LLRVAHLGTG RRILYKYRRQ
NKMAEILYDS TRVSFTYDET AGVLKTVNLQ SEGFICSIRY RQIGPLVDRQ IFRFSEDGMV
NARFDYTYDN SFRVTSMQAV INETPLPIDL YQFDDISGKV EQFGKFGVIY YDINQIISTA
VMTYTKHFDV HGRIKEIQYE IFRSLMYWIT IQYDNMGRVT KREIKIGPFA NTTKYGYEYD
VDGQLQTVYL NEKMMWRYNY DLNGNLHLLN PGNSARLTPL RYDLRDRITR LGDVQYRLDD
DGFLRQRGAE IFEYNSKGLL ERVYSKGNSW TIQYRYDGLG RRVASRTSLG QHLQFFYADL
NYPTRITHVY NHSSSEITSL YYDLQGHLFA MEISSGEEFY IACDNTGTPL AVFSSNGLLL
KQVQYTAYGE VYFDSNPDFV LVIGFHGGLY DPLTRLLHFG DRDYDIPAGR WTTPDIGTWT
RVGKDPAPFN LYMFRNNNPV SKVHEVKEYV TDVNIWLVTF GFHLHNAIPG FPIPKFDLTQ
PSLEMKKSQL WDDLPSISGV QQEVTRQAKA FLSFERMPEI QLSRRHSNRE KPWLWFATAK
SLIGKGVMLA VTQGRVVTNT LNIANEDCIK VAAVLNNAFY LEDLHFTVEG RDTHYFIKTS
LPESDLGALR LTSGRKSLEN GVNVTVSQST TVVNGRTRRF ADVELQYGAL ALHVRYGMTL
DEEKARVLEQ ARQKALASAW SREQQRVREG EEGVRLWTEG EKRQLLSGGK VLGYDGYYVL
SIEQYPELAD SANNIQFLRQ SEIGKR
//