ID A0A1S3SSV1_SALSA Unreviewed; 2722 AA.
AC A0A1S3SSV1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Teneurin-3-like isoform X2 {ECO:0000313|RefSeq:XP_014067415.1};
GN Name=LOC106611581 {ECO:0000313|RefSeq:XP_014067415.1};
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_014067415.1};
RN [1] {ECO:0000313|RefSeq:XP_014067415.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014067415.1};
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_014067415.1; XM_014211940.1.
DR GeneID; 106611581; -.
DR OrthoDB; 5491728at2759; -.
DR Proteomes; UP000087266; Chromosome ssa09.
DR Bgee; ENSSSAG00000070557; Expressed in brain and 5 other cell types or tissues.
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 Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.10.25.10; Laminin; 4.
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:SF63; TENEURIN-3 ISOFORM X1; 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 PROSITE; PS00022; EGF_1; 4.
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: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 313..338
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 2..313
FT /note="Teneurin N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51361"
FT DOMAIN 759..794
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 118..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 763..773
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 784..793
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 2722 AA; 302749 MW; 819F487A9171AACB CRC64;
MEQVKEQRPF CSLSKSQRDH ERERDLERRY TASSTDREGA CRVPTQKSYS SSETLQAYDH
DPARLLFSGR VKEMAYQETN DYGRPGQGFS LRQLGICEPS TRRGLALCPE TGLSHPLGRY
SRRTVPTENH EPTSPERTMA LWGRGAKSGQ SSCLSSRSNS ALTITDTEID NKSDNEIEDR
LSSQQGQPPL PPDTPTHHKQ HPSITSLSRG SLANQRSLSP PPSAGLAAEL QSTAECVQLQ
DSWVLDSNVA LESRHFLFKT GTGTTPFFST PTPGYTMATG AVYSTPARPL PRNNLSRGAF
KLKKSPKHCS WRCTALSAVG VAVLLSIILC YCIAMHFFGL NWQLQETENQ PTFENGGVKT
LPTQPNILTP LSADYGRNGA AHQENSSVDT GQVEVGRRVS QGIPPGVFWR SRLAMEHPRF
LKFNISVQKN ALVGVYGRKG LPPSHTQYDF VELLDGSKLI AKERRASTEP EARGQMEHQV
SLHQAGFIQY LDSGVWHLAF YNDGKRPETV SYNTIILESV MECSHNCYGN GECVSGSCHC
FPRFSGPYCS RAACPILCSG NGQYARGRCQ CYSGWKGTEC DVPATQCVDP QCGGHGICVT
GNCVCNAGHK GSNCHQVDCL DPTCSGHGSC HHGECHCNPG WGGMGCAILR STCPEQCSSH
GTFHTETGTC ICEANWTGTD CSVEVCTVDC GPHGACVSGT CHCEEGSAGS ECDQRDCHPR
CTDHGVCREG KCDCHQGWTG EHCAIALDSR VSGAVKIGYK DGCPGLCNSN GRCILDQAGW
RCICQSGWRG LGCDVATETF CSDGKDNERD GLVDCMDPDC CSQSSCQGQP YCHGSPDPIS
IVSQGQGSSS TQSAPRGFYE RISFLVGHGG SHVIPGDNPF NSSLVSIIRG QVLTGDGTPL
IGVNVSFRDY PEYGYTVTRQ DGMFDLLANG GASLTLSLKR DPFPTLHRTV WLPWKVFHVM
DTVMMTRENN NIPSCHLIGL LRPSPLILAS PLSTFYRSSP KDSPIIPETQ VLHEEVAIPG
SDLNLVYLSS RTSGYKPILK VLMTQERLPF GLMKVHLMVA VMGRLFQKSL PAFPDLSYTF
VWDKTDAYNQ KVYGLSEAVV SVGYEYESCL DVILWEKRTA ILQGYELDAS NMGGWMLDKH
HILDIQNGIL FKGSGENQFI SLQPPVISTV MGNGRRRSIS CPSCNGQALG NKLLAPLALA
WGIDGSLYVG DFNYIRRVYP SGNVTSVMEL SNNPAHRYYL ATDPVTGQLY VSDTYSRRIY
RPKVLTGIKE LQSNAEVVAG TGEHCLPFDE THCGDGAKAT EALLTGPKGI AVDKNGLIYF
VDGTTIRRVD QNGIISTLLG SNDLTSARPL TCDISMEINQ VLLEWPTDLA VSPMDNSLYI
LDNNVVLRIT ENGQVSIAAG RPIHCPLAGM DRGAARGQRA ALTPLESAVA IAVSYYGAIY
VAETDERKLS RIRTISVDGE ITHLAGSPSD CDCKNDVNCD CYQTGEGYAK DARLNVPSSL
VVAPDGTLYV ADLGNIRIRA VSRNGPVLTS NTNTFEVASP DAQEVYVFDA NGTHQHTSSL
LTGDFKYTFS YSIENDVTAV TDSNGNTLRI RRDPNRMPVR IVAPDNQVIW LIMGTNGGLK
TLTAQGQELV LLTYHGNTGL LATKTSEIGW TTFYEYDSEG RIMNVTFPTG TVKNLYTEID
RALTVDIESS LTEEEISITT NTSTIRAFYT LAQDQCRSSY QVGYDNSLRI TYANGMDTHY
QTEPHILAGT AIPTVARRNM SLPGESGQNL VEWRFRKEQA RGKVIVFGRK LRVNGRNILS
VDYDRTLRTE KIYDDHRKFL LKIIYDGTGH PVLWVPSSKL LPVNVSLSSN GQINALQRGP
TTERLEYDSQ GRLVSRVFAD GKRWSYTYLD KSMVLLLHSQ RQYIFDFDSQ DRLSAVTMPS
VARYTMQTVR SVGYYRNLFH PPDSNASVAV DYSEDGLLQR VAHLGTGRQV LYKYRRQNKL
AEVLYDITRV SFTYDEMAGV LKTVNLQSEG FICSIRYRQV GPLVDRQIFR FSEDGMVNAR
FDYTYDSSLR ITSVQGVINE TPLPIDLYQF DDISGKVEQF GKFGVIYYDI NQIISTAVMT
YTKHFDAHGR IKEIQYEIFR SLMYWITFQY DDTGRCTKRE IKIGPFANTT QYGYEYDVDG
QLQTVYLNDK VMWRYTYDLN GNLHLLNPGN GARLLPLRYD LRDRITRLGD IQYRMDEDGF
LRQRGSEIFE YNSKGLLARV YSKSNGWIIQ YRYDGLGRRV STKASLGQYL QYFYADLSYP
SRITHVYNHS SSEITSLYYD LQGHLFAQEI SSGEEYYIAC DNTGTPLAVF TSNGLLIKQV
QYTAYGEIYF DSNPDFQLVL GFHGGLYDPL TKLLHFGERD YDIMPGRWTV PDISTWKRVG
KEPGPFNLYM FRNNNPISKV HEVREYVEDV NSWLVTFGFH LHNTIPGFPV PKFDLTHPSY
ELKKSQLWDD LPSISGVQQE VTRQAHALLS FERLPEVHAG RGRRGERPWF WFSAAQSLIG
RAVMFAIYKG TAHTHTLNVA NEDCIKVAAV LNNAFYLENL HFTVEGRDTH YFVKPGVPDG
DLAALRLTSG HKTLENGVNV SVSQSTTVMD SRTRRFADVE LGRGPLALHV RYGSTVDEEK
ARVLELARQR ALVSAWANEQ QRVSDGEEGV RPWTEGEKRQ LLSSGKVQGY DGYYVLSIEL
YPELADSAKN IQFLRQSEIG KR
//
