TENSH_CAEEL
ID TENSH_CAEEL Reviewed; 1354 AA.
AC H2L045; A0A0S4XR26; A0A0S4XR31; A0A0S4XR51; A0A0S4XR69; H2L046; H2L047;
AC P92160;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 17-FEB-2016, sequence version 2.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Tensin homolog {ECO:0000312|WormBase:M01E11.7a};
DE EC=3.1.3.48 {ECO:0000250|UniProtKB:Q63HR2};
DE AltName: Full=C1 domain-containing phosphatase and tensin homolog {ECO:0000305};
DE AltName: Full=Suppressor of vhp-1 deletion lethality protein svh-6 {ECO:0000303|PubMed:31109965};
GN Name=tns-1 {ECO:0000312|WormBase:M01E11.7a};
GN Synonyms=svh-6 {ECO:0000303|PubMed:31109965},
GN tag-163 {ECO:0000312|WormBase:M01E11.7a};
GN ORFNames=M01E11.7 {ECO:0000312|WormBase:M01E11.7a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, INTERACTION WITH SVH-2 AND PAT-3, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND MUTAGENESIS OF 38-MET--SER-335; ARG-1108 AND
RP 1192-ALA--SER-1354.
RX PubMed=31109965; DOI=10.1523/jneurosci.2059-18.2019;
RA Hisamoto N., Shimizu T., Asai K., Sakai Y., Pastuhov S.I., Hanafusa H.,
RA Matsumoto K.;
RT "C. elegans Tensin Promotes Axon Regeneration by Linking the Met-like SVH-2
RT and Integrin Signaling Pathways.";
RL J. Neurosci. 39:5662-5672(2019).
CC -!- FUNCTION: Probable phosphatase which regulates axon regeneration after
CC injury by linking the svh-2 and integrin signaling pathways.
CC {ECO:0000269|PubMed:31109965}.
CC -!- FUNCTION: [Isoform e]: Not involved in axon regeneration after injury.
CC {ECO:0000269|PubMed:31109965}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48;
CC Evidence={ECO:0000250|UniProtKB:Q63HR2};
CC -!- SUBUNIT: May interact (via SH2 domain) with receptor svh-2 (when
CC tyrosine-phosphorylated) (PubMed:31109965). May interact (via C-
CC terminus) with integrin pat-3 (PubMed:31109965).
CC {ECO:0000269|PubMed:31109965}.
CC -!- SUBCELLULAR LOCATION: Cell projection, axon
CC {ECO:0000269|PubMed:31109965}. Note=Localizes to punctate structures
CC along the axon in motor neurons. {ECO:0000269|PubMed:31109965}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Name=a {ECO:0000312|WormBase:M01E11.7a};
CC IsoId=H2L045-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:M01E11.7b}; Synonyms=tns-1s
CC {ECO:0000303|PubMed:31109965};
CC IsoId=H2L045-2; Sequence=VSP_060492;
CC Name=c {ECO:0000312|WormBase:M01E11.7c};
CC IsoId=H2L045-3; Sequence=VSP_060502;
CC Name=d {ECO:0000312|WormBase:M01E11.7d};
CC IsoId=H2L045-4; Sequence=VSP_060502, VSP_060504, VSP_060505;
CC Name=e {ECO:0000312|WormBase:M01E11.7e};
CC IsoId=H2L045-5; Sequence=VSP_060503;
CC Name=f {ECO:0000312|WormBase:M01E11.7f};
CC IsoId=H2L045-6; Sequence=VSP_060501;
CC Name=g {ECO:0000312|WormBase:M01E11.7g};
CC IsoId=H2L045-7; Sequence=VSP_060500;
CC Name=h {ECO:0000312|WormBase:M01E11.7h};
CC IsoId=H2L045-8; Sequence=VSP_060499;
CC -!- TISSUE SPECIFICITY: Expressed in ventral motor neurons, including
CC ventral and dorsal D-type neurons, and in a subset of cells in the
CC head. {ECO:0000269|PubMed:31109965}.
CC -!- SIMILARITY: Belongs to the PTEN phosphatase protein family.
CC {ECO:0000305}.
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DR EMBL; BX284601; CCD71346.2; -; Genomic_DNA.
DR EMBL; BX284601; CCD71347.1; -; Genomic_DNA.
DR EMBL; BX284601; CCD71348.1; -; Genomic_DNA.
DR EMBL; BX284601; CCD71349.1; -; Genomic_DNA.
DR EMBL; BX284601; CUV67053.1; -; Genomic_DNA.
DR EMBL; BX284601; CUV67056.1; -; Genomic_DNA.
DR EMBL; BX284601; CUV67057.1; -; Genomic_DNA.
DR EMBL; BX284601; CUV67058.1; -; Genomic_DNA.
DR PIR; T29328; T29328.
DR RefSeq; NP_001305199.1; NM_001318270.1. [H2L045-5]
DR RefSeq; NP_001305202.1; NM_001318273.1. [H2L045-6]
DR RefSeq; NP_001305203.1; NM_001318274.1. [H2L045-7]
DR RefSeq; NP_001305204.1; NM_001318275.1. [H2L045-8]
DR RefSeq; NP_491636.1; NM_059235.3.
DR RefSeq; NP_491637.2; NM_059236.4. [H2L045-1]
DR RefSeq; NP_491638.1; NM_059237.6. [H2L045-2]
DR RefSeq; NP_740854.1; NM_170867.3. [H2L045-4]
DR AlphaFoldDB; H2L045; -.
DR SMR; H2L045; -.
DR IntAct; H2L045; 7.
DR STRING; 6239.F46F11.3; -.
DR EPD; H2L045; -.
DR PeptideAtlas; H2L045; -.
DR EnsemblMetazoa; M01E11.7a.1; M01E11.7a.1; WBGene00006508. [H2L045-1]
DR EnsemblMetazoa; M01E11.7b.1; M01E11.7b.1; WBGene00006508. [H2L045-2]
DR EnsemblMetazoa; M01E11.7c.1; M01E11.7c.1; WBGene00006508. [H2L045-3]
DR EnsemblMetazoa; M01E11.7c.2; M01E11.7c.2; WBGene00006508. [H2L045-3]
DR EnsemblMetazoa; M01E11.7c.3; M01E11.7c.3; WBGene00006508. [H2L045-3]
DR EnsemblMetazoa; M01E11.7d.1; M01E11.7d.1; WBGene00006508. [H2L045-4]
DR EnsemblMetazoa; M01E11.7e.1; M01E11.7e.1; WBGene00006508. [H2L045-5]
DR EnsemblMetazoa; M01E11.7f.1; M01E11.7f.1; WBGene00006508. [H2L045-6]
DR EnsemblMetazoa; M01E11.7g.1; M01E11.7g.1; WBGene00006508. [H2L045-7]
DR EnsemblMetazoa; M01E11.7h.1; M01E11.7h.1; WBGene00006508. [H2L045-8]
DR GeneID; 172215; -.
DR KEGG; cel:CELE_M01E11.7; -.
DR UCSC; M01E11.7c; c. elegans.
DR CTD; 172215; -.
DR WormBase; M01E11.7a; CE51166; WBGene00006508; tns-1. [H2L045-1]
DR WormBase; M01E11.7b; CE12302; WBGene00006508; tns-1. [H2L045-2]
DR WormBase; M01E11.7c; CE28613; WBGene00006508; tns-1. [H2L045-3]
DR WormBase; M01E11.7d; CE30558; WBGene00006508; tns-1. [H2L045-4]
DR WormBase; M01E11.7e; CE51160; WBGene00006508; tns-1. [H2L045-5]
DR WormBase; M01E11.7f; CE51213; WBGene00006508; tns-1. [H2L045-6]
DR WormBase; M01E11.7g; CE51205; WBGene00006508; tns-1. [H2L045-7]
DR WormBase; M01E11.7h; CE51229; WBGene00006508; tns-1. [H2L045-8]
DR eggNOG; KOG1930; Eukaryota.
DR GeneTree; ENSGT00940000163886; -.
DR HOGENOM; CLU_009407_0_0_1; -.
DR InParanoid; H2L045; -.
DR OrthoDB; 172407at2759; -.
DR PRO; PR:H2L045; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00006508; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0030424; C:axon; IDA:UniProtKB.
DR GO; GO:0030054; C:cell junction; HDA:WormBase.
DR GO; GO:0005925; C:focal adhesion; IBA:GO_Central.
DR GO; GO:0031430; C:M band; HDA:WormBase.
DR GO; GO:0055120; C:striated muscle dense body; HDA:WormBase.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0048680; P:positive regulation of axon regeneration; IDA:UniProtKB.
DR CDD; cd01213; PTB_tensin; 1.
DR CDD; cd09927; SH2_Tensin_like; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.30.505.10; -; 1.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR013625; PTB.
DR InterPro; IPR006020; PTB/PI_dom.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR035012; Tensin-like_SH2.
DR InterPro; IPR014020; Tensin_C2-dom.
DR InterPro; IPR033929; Tensin_PTB.
DR Pfam; PF08416; PTB; 1.
DR Pfam; PF10409; PTEN_C2; 1.
DR Pfam; PF00017; SH2; 1.
DR SMART; SM00462; PTB; 1.
DR SMART; SM01326; PTEN_C2; 1.
DR SMART; SM00252; SH2; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR PROSITE; PS51182; C2_TENSIN; 1.
DR PROSITE; PS51181; PPASE_TENSIN; 1.
DR PROSITE; PS50001; SH2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Hydrolase; Protein phosphatase;
KW Reference proteome; SH2 domain.
FT CHAIN 1..1354
FT /note="Tensin homolog"
FT /id="PRO_0000449098"
FT DOMAIN 38..207
FT /note="Phosphatase tensin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00590"
FT DOMAIN 212..337
FT /note="C2 tensin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00589"
FT DOMAIN 1083..1187
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT REGION 380..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 597..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 638..660
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 692..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 734..754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 794..879
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1015..1035
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 820..847
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 144
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00590"
FT VAR_SEQ 1..1095
FT /note="Missing (in isoform h)"
FT /evidence="ECO:0000305"
FT /id="VSP_060499"
FT VAR_SEQ 1..1063
FT /note="MAAAALCCASRKSNKYNNEAGYEVYTISEDQLRLKQKMKDRKEGVQVEYITS
FT RLIVLSCTSETSERKFVESLLKASQQIQNAHNKHIRVWNVSQRRHDISSSLDAIPFGWP
FT SETAPSLEKLCTICKNLDQWMLEHPLNIAVIFCKGGLERCAIVVNAFMRFNAISATDDS
FT VDDRFSMQRFSERFLGPDGPPSYKRYLGYFSSLLSGRISVNSDPLYLHNIILTFFEPIN
FT VFLKIYERLVPVYQSKTVALNKSSKFEMDGSLKLRGDIFFKCIVAASSPGSSTRCLFTC
FT QLNTCALELHPINSEGYSVVRLHKEELDLIFNDKKIDNRVTVELVVSHTSGPTTIATAA
FT VQSVHSLLPRNNSYETFELAQDDETNRSRLEVEYSEIRKKSTKSSKSANPINNNQEEEM
FT PVGPPVPPKPSTPIMNGERLGEYGVGGHIGNGDVVPERRGILPASLREKINQKKELEGR
FT ATPSIEPDLVGRDRYDKASRCFSYVPAKSMQEAFERPRRTSFSRAIEKRENSVENVSQE
FT EVARTEIPQSYQQNDISTPAKWDEQVEDAKQSALLEELARAPSAMQHNYWGNGEVDNVQ
FT VVDQAQRAVITPTSTLQRRPKPPARSGSYRTLNDDAYCSDMDELCDPEYYLNYNSNTAP
FT LPPPRRQEQHAGTRSVQLPRKKMNFDAVTDPLDDVLESTKRLGSAYSVGDVRGGQQQQQ
FT EQHNASNDFNFSNTLNNTPTDYRQHYRNRNCQSVTTPRNHHFSTPSREQEADAADTWLS
FT GKLKKVRSKRDIDPDIVRRRTQEKMLLEELKDSAANNDENQHNLPNGHARGAGLQNIDP
FT LAEFRREEERLRNTRSPYGEERWRGRMRGKPPTPPPRESSASPVNSLPRGTPAHHMDRQ
FT RHNQSVPLPMHHRQFDEDFDVNSLFNFSHDPRQQSTTLERGGRSLSRGARIQDAYYASQ
FT QDLSANNRFNSGQERVAAAIYRAETAHRDMYASGTINRAETPGRYFPENSAVLERSSTP
FT SFPVSRATPLPFHPLLYNNGERGGSGHAAGGGGGGHNGYSTMNNRSASPRLFGGSSTLS
FT RRSSVNSV -> MSDTATTSTTVVIHLKRSNHDDASASATTAQLQQRSRYCDVSLASSE
FT ESSDLSDAEEKDDLIRRTITSSSKDTMEEGDDDDEEEFDDVVMEEDVGGGTDANEQFSR
FT VIQRQISGAGGGILKKSNGK (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_060492"
FT VAR_SEQ 1..1037
FT /note="Missing (in isoform g)"
FT /evidence="ECO:0000305"
FT /id="VSP_060500"
FT VAR_SEQ 1..784
FT /note="Missing (in isoform f)"
FT /evidence="ECO:0000305"
FT /id="VSP_060501"
FT VAR_SEQ 1..405
FT /note="Missing (in isoform c and isoform d)"
FT /evidence="ECO:0000305"
FT /id="VSP_060502"
FT VAR_SEQ 1..37
FT /note="Missing (in isoform e)"
FT /evidence="ECO:0000305"
FT /id="VSP_060503"
FT VAR_SEQ 1065..1069
FT /note="TSEII -> GRSYL (in isoform d)"
FT /evidence="ECO:0000305"
FT /id="VSP_060504"
FT VAR_SEQ 1070..1354
FT /note="Missing (in isoform d)"
FT /evidence="ECO:0000305"
FT /id="VSP_060505"
FT MUTAGEN 38..335
FT /note="Missing: Does not impair axon regeneration after
FT injury."
FT /evidence="ECO:0000269|PubMed:31109965"
FT MUTAGEN 1108
FT /note="R->K: Impairs axon regeneration after injury."
FT /evidence="ECO:0000269|PubMed:31109965"
FT MUTAGEN 1192..1354
FT /note="Missing: Impairs axon regeneration after injury."
FT /evidence="ECO:0000269|PubMed:31109965"
SQ SEQUENCE 1354 AA; 151404 MW; 9D67B6BBB0E59965 CRC64;
MAAAALCCAS RKSNKYNNEA GYEVYTISED QLRLKQKMKD RKEGVQVEYI TSRLIVLSCT
SETSERKFVE SLLKASQQIQ NAHNKHIRVW NVSQRRHDIS SSLDAIPFGW PSETAPSLEK
LCTICKNLDQ WMLEHPLNIA VIFCKGGLER CAIVVNAFMR FNAISATDDS VDDRFSMQRF
SERFLGPDGP PSYKRYLGYF SSLLSGRISV NSDPLYLHNI ILTFFEPINV FLKIYERLVP
VYQSKTVALN KSSKFEMDGS LKLRGDIFFK CIVAASSPGS STRCLFTCQL NTCALELHPI
NSEGYSVVRL HKEELDLIFN DKKIDNRVTV ELVVSHTSGP TTIATAAVQS VHSLLPRNNS
YETFELAQDD ETNRSRLEVE YSEIRKKSTK SSKSANPINN NQEEEMPVGP PVPPKPSTPI
MNGERLGEYG VGGHIGNGDV VPERRGILPA SLREKINQKK ELEGRATPSI EPDLVGRDRY
DKASRCFSYV PAKSMQEAFE RPRRTSFSRA IEKRENSVEN VSQEEVARTE IPQSYQQNDI
STPAKWDEQV EDAKQSALLE ELARAPSAMQ HNYWGNGEVD NVQVVDQAQR AVITPTSTLQ
RRPKPPARSG SYRTLNDDAY CSDMDELCDP EYYLNYNSNT APLPPPRRQE QHAGTRSVQL
PRKKMNFDAV TDPLDDVLES TKRLGSAYSV GDVRGGQQQQ QEQHNASNDF NFSNTLNNTP
TDYRQHYRNR NCQSVTTPRN HHFSTPSREQ EADAADTWLS GKLKKVRSKR DIDPDIVRRR
TQEKMLLEEL KDSAANNDEN QHNLPNGHAR GAGLQNIDPL AEFRREEERL RNTRSPYGEE
RWRGRMRGKP PTPPPRESSA SPVNSLPRGT PAHHMDRQRH NQSVPLPMHH RQFDEDFDVN
SLFNFSHDPR QQSTTLERGG RSLSRGARIQ DAYYASQQDL SANNRFNSGQ ERVAAAIYRA
ETAHRDMYAS GTINRAETPG RYFPENSAVL ERSSTPSFPV SRATPLPFHP LLYNNGERGG
SGHAAGGGGG GHNGYSTMNN RSASPRLFGG SSTLSRRSSV NSVDTSEIIH HHPLFVKDTS
KYWYKPTISR EQAINMLRDK PPGTFVVRDS NSFPGAFGLA LKVSTPPPGV NPGDGSELVR
HFLIEPSPKG VKLKGCNNEP VFGSLSALVY QHSITALALP TKLVLPDFDP AATPEHLSAT
QALLEQGAAC NVVYVGSVDV ESLTGNECVK RSIATCSQRA INGDSRAVSV HFKVSSQGVT
LTDNTRKVFF RRHFNVQSVI FAGMDPIERR FENTRALGFH DGCIAQARLF AFVARIPSSS
ENACHVFAEL EPEQPGSAVV NFINKVMLAQ KNRS