ID A0A1S3RFC4_SALSA Unreviewed; 2785 AA.
AC A0A1S3RFC4;
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 X13 {ECO:0000313|RefSeq:XP_014050572.1};
GN Name=LOC106602442 {ECO:0000313|RefSeq:XP_014050572.1};
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_014050572.1};
RN [1] {ECO:0000313|RefSeq:XP_014050572.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014050572.1};
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_014050572.1; XM_014195097.1.
DR OrthoDB; 5491728at2759; -.
DR Proteomes; UP000087266; Chromosome ssa04.
DR Bgee; ENSSSAG00000056252; Expressed in sexually immature organism and 11 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 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; 2.
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; 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; 2.
DR PROSITE; PS00022; EGF_1; 4.
DR PROSITE; PS01186; EGF_2; 3.
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 391..416
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..391
FT /note="Teneurin N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51361"
FT DOMAIN 691..723
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 725..758
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 820..855
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..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 251..305
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 178..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 713..722
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 748..757
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 824..834
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 845..854
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 2785 AA; 309905 MW; 0C04026398945256 CRC64;
MDVKERRPYC SLTKSRRDKE RRYTGSSGDS EECGSGGPGP RVPTQKSYSS SETLKAFDHQ
DSSRLLYSSR VKEMVHREQD EYTRQGQNFN LRQLGICEPS TRRGLAFCAE MGLPHRGYSV
GAGSDVDPEN EGVMSPERAM RLWGRGVKSG GRNSCLSSRS NSALTLTDTE HENKSDSDNG
SPMPSSLPSP SVTDHSHSQP PSPNLHDNQS SLLSSASAHP AVHESDEDEE EYTATLYLPV
TQVTAHSHHG LACNEQPSNH HQQGQSTLPP APPPHKQQPS VTALNHNSLS SRNRNPSPAP
PAALPAELQT TPESVPLQDS WVLGSNVPLE SRHFLFKTGT GTTPLFSTAT PGYTMATGSV
YSPPTRPLPR NTLSRSAFKF KKSSKYCSWR CTALSAVGLS VLLSVLLCYC IAMHLFGLNW
QLQETEGYTF ENGLGRSDTT PNTITALSAD NGKLGVFLQE NNTIDTGEVD VGRRAVQEVP
PGIFWRSQLY IDQPQFLKFN ISVQRDALVG VYGRKGLPPS HTQYDFVELL DGSRLITKEK
RGLVEVEGVS RRARSVSVHE AGFIQYLDSG IWHMAFYNDG KNSEQVSYNT IVIESVMECP
HNCHGNGDCL SGTCHCFPGF LGPDCSRASC PVLCSGNGQY SRGRCLCFSG WKGTECDVPS
NQCIDIHCGG HGICIIGVCV CNTRYKGDNC EEVDCLDPGC SAHGVCIHGE CHCSPGWGGT
NCEILKTMCP DQCSGHGTYQ SESGTCTCDT NWTGPDCSIE VCVVDCGSNG VCFGGSCRCE
EGWTGTVCDQ KACHPMCTKN GVCKEGKCEC NQGWTGEHCN IEGCPGLCNN NGRCTLDQNG
WHCVCQSGWR GAGCDVAMET LCTDGKDNEG DGLADCMDPD CCLQTSCQTQ PYCRGSPDPS
EIISQSPSSL MPQHAARSFY QRIRFLVGPE GSHVITGDNP FNKSLVSIIR GQVLTADGTP
LIGVNVTFVH YPDHGYTITR KDGMFDLLTN GGASLTLSFE RAPFLIQYHT VWIPWNVFYV
IDTLVMKKEE NDIPSCDLSG FIRPSPVIVA SPLSTCFRSS PEDGPIIPET QVLQEETSIP
GSDLNLLYLS SRAAGYKPVL KVTMTQASVP FNLMKVHLMV AVVGRLFQKW FPAQPNLSYT
FIWDKTDAYN QKVYGLSEAV VSVGFEYESC LDLILWEKRT ATLQGYELDA SNMGGWTLDK
HHILDIQNGI LYKGNGENVF ISQQPPVISS IMGNGRRRSI SCPSCNGQAE GNKLLAPVAL
ACGADGSLFV GDFNYIRRIF PSGNVTSVME LSNNPAHRYY LATDPVTGQL YVSDTNSRRI
YRPKVLTGTK ELIQNGEVVA GTGEQCPPFD EARCGDGGKA TEALLMGPKG ITVDKNGYIY
FVDGTMIRKV DRNGIISTLL GSNDLTSARP LTCDTSMHIR QVRLEWPTAL AINPMDNSIY
VLDNNVVLQI TENRQVRIVA GRPMHCQVPG IEYMLGKRAV QTMLEGAAAI ALSYSGVLYI
AETDEKKIHR IRQVSTDGEI TPLAGALSDC DCKNDANCDC YQTGDGYAKD ARLNSPSSLV
VSPDGTLYVA DLGNIRIRAV RRNQPPSGSA VSGPGSFEVA SPSSQELYVF DSNGTHQFTM
SLVTGDYKYN FSYSNEEDVT AVTDSSGNTL RIRRDPNRMP VRIVAPDNQV IWLTIGTNGG
LKTLTAQGQE LVLFTYHGNS GLLATKTIQI GWTTFYDYDS EGRLTNVTFP TGVVTNLHGD
MTGAITVDIE TSGRDEDVSI TTNLSSIDSF YTLVQDQLRN SYQVGYDHSL RVIYANGMDT
HYQTEPHILA GAANPTVARR NMTLPGENGQ NLVEWRFRKE QTRGKVIVFG RKLRVNGRNL
LSVDYDRTLR TEKIYDDHRK FLLKIVYDTQ GHPTLWVPSS KLLSVNLTYS STGQVTSLQR
GPTTERVEYD GQGRIVSRVF ADGKTWSFTY LDKSMVLLLH SQRQYIFDYD LLDRLSAVTM
PSVARHTMQT IRSLGYYRNI YNPPESNASV TVDYSEDGQL LRVAHLGTGR RILYKYRRQN
KMAEILYDST RVSFTYDETA GVLKTVNLQS EGFICSIRYR QIGPLVDRQI FRFSEDGMVN
ARFDYTYDNS FRVTSMQAVI NETPLPIDLY QFDDISGKVE QFGKFGVIYY DINQIISTAV
MTYTKHFDVH GRIKEIQYEI FRSLMYWITI QYDNMGRVTK REIKIGPFAN TTKYGYEYDV
DGQLQTVYLN EKMMWRYNYD LNGNLHLLNP GNSARLTPLR YDLRDRITRL GDVQYRLDDD
GFLRQRGAEI FEYNSKGLLE RVYSKGNSWT IQYRYDGLGR RVASRTSLGQ HLQFFYADLN
YPTRITHVYN HSSSEITSLY YDLQGHLFAM EISSGEEFYI ACDNTGTPLA VFSSNGLLLK
QVQYTAYGEV YFDSNPDFVL VIGFHGGLYD PLTRLLHFGD RDYDIPAGRW TTPDIGTWTR
VGKDPAPFNL YMFRNNNPVS KVHEVKEYVT DVNIWLVTFG FHLHNAIPGF PIPKFDLTQP
SLEMKKSQLW DDLPSISGVQ QEVTRQAKAF LSFERMPEIQ LSRRHSNREK PWLWFATAKS
LIGKGVMLAV TQGRVVTNTL NIANEDCIKV AAVLNNAFYL EDLHFTVEGR DTHYFIKTSL
PESDLGALRL TSGRKSLENG VNVTVSQSTT VVNGRTRRFA DVELQYGALA LHVRYGMTLD
EEKARVLEQA RQKALASAWS REQQRVREGE EGVRLWTEGE KRQLLSGGKV LGYDGYYVLS
IEQYPELADS ANNIQFLRQS EIGKR
//
