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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
 
 
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