PTRN1_CAEEL
ID PTRN1_CAEEL Reviewed; 1112 AA.
AC U4PAZ9; Q966J8; U4PLF6; W6SB68;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 11-DEC-2013, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Patronin (microtubule-binding protein) homolog {ECO:0000312|WormBase:F35B3.5c};
GN Name=ptrn-1 {ECO:0000312|WormBase:F35B3.5c};
GN ORFNames=F35B3.5 {ECO:0000312|WormBase:F35B3.5c};
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|EMBL:CDH92934.1,
RC 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, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=25437544; DOI=10.1016/j.celrep.2014.09.054;
RA Chuang M., Goncharov A., Wang S., Oegema K., Jin Y., Chisholm A.D.;
RT "The microtubule minus-end-binding protein patronin/PTRN-1 is required for
RT axon regeneration in C. elegans.";
RL Cell Rep. 9:874-883(2014).
RN [3] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=24569477; DOI=10.7554/elife.01498;
RA Richardson C.E., Spilker K.A., Cueva J.G., Perrino J., Goodman M.B.,
RA Shen K.;
RT "PTRN-1, a microtubule minus end-binding CAMSAP homolog, promotes
RT microtubule function in Caenorhabditis elegans neurons.";
RL Elife 3:E01498-E01498(2014).
RN [4] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=24569480; DOI=10.7554/elife.01637;
RA Marcette J.D., Chen J.J., Nonet M.L.;
RT "The Caenorhabditis elegans microtubule minus-end binding homolog PTRN-1
RT stabilizes synapses and neurites.";
RL Elife 3:E01637-E01637(2014).
RN [5] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=26371552; DOI=10.7554/elife.08649;
RA Wang S., Wu D., Quintin S., Green R.A., Cheerambathur D.K., Ochoa S.D.,
RA Desai A., Oegema K.;
RT "NOCA-1 Functions with gamma-tubulin and in parallel to Patronin to
RT assemble non-centrosomal microtubule arrays in C. elegans.";
RL Elife 4:E08649-E08649(2015).
RN [6]
RP FUNCTION, INTERACTION WITH DAPK-1, SUBCELLULAR LOCATION, DOMAIN, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=27661253; DOI=10.7554/elife.15833;
RA Chuang M., Hsiao T.I., Tong A., Xu S., Chisholm A.D.;
RT "DAPK interacts with Patronin and the microtubule cytoskeleton in epidermal
RT development and wound repair.";
RL Elife 5:E15833-E15833(2016).
CC -!- FUNCTION: Required for microtubule stability and anchorage by binding
CC to the minus ends of microtubules (PubMed:25437544, PubMed:26371552,
CC PubMed:27661253). Acts redundantly with noca-1 to control
CC circumferential microtubule assembly along the body which is necessary
CC for larval development, viability, morphology and integrity of the
CC epidermis (PubMed:26371552). Promotes microtubule stability and
CC polymerization in neurons (PubMed:24569477). Involved in the
CC maintenance of neurite morphology in ALM and PLM neurons
CC (PubMed:25437544, PubMed:24569477, PubMed:24569480). May play a role in
CC synaptic protein localization in the PLM neuron (PubMed:24569477). May
CC act upstream of dlk-1 in neuronal regeneration (PubMed:25437544,
CC PubMed:24569480). Plays a role in postembryonic epidermal tissue
CC integrity and wound healing (PubMed:27661253).
CC {ECO:0000269|PubMed:24569477, ECO:0000269|PubMed:24569480,
CC ECO:0000269|PubMed:25437544, ECO:0000269|PubMed:26371552,
CC ECO:0000269|PubMed:27661253}.
CC -!- SUBUNIT: Interacts with dapk-1. {ECO:0000269|PubMed:27661253}.
CC -!- SUBCELLULAR LOCATION: Cell projection, axon
CC {ECO:0000269|PubMed:24569477, ECO:0000269|PubMed:25437544}. Cell
CC projection, dendrite {ECO:0000269|PubMed:24569477,
CC ECO:0000269|PubMed:24569480, ECO:0000269|PubMed:25437544}. Cell
CC membrane, sarcolemma {ECO:0000269|PubMed:24569477}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:24569477, ECO:0000269|PubMed:27661253}. Cytoplasm,
CC cytoskeleton {ECO:0000269|PubMed:24569477,
CC ECO:0000269|PubMed:27661253}. Perikaryon {ECO:0000269|PubMed:24569480}.
CC Note=Localizes to puncta throughout the dendrites and axon of neurites,
CC within the cytosol of muscle cells and at the sarcolemma
CC (PubMed:24569477). Expressed in puncta along the dendrites of neurons
CC and in the perikaryon (PubMed:25437544, PubMed:24569480). Localizes
CC along microtubules (PubMed:27661253). {ECO:0000269|PubMed:24569477,
CC ECO:0000269|PubMed:24569480, ECO:0000269|PubMed:25437544,
CC ECO:0000269|PubMed:27661253}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=c {ECO:0000312|WormBase:F35B3.5c};
CC IsoId=U4PAZ9-1; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:F35B3.5a};
CC IsoId=U4PAZ9-2; Sequence=VSP_058273;
CC Name=d {ECO:0000312|WormBase:F35B3.5d};
CC IsoId=U4PAZ9-3; Sequence=VSP_058271;
CC Name=e {ECO:0000312|WormBase:F35B3.5e};
CC IsoId=U4PAZ9-4; Sequence=VSP_058272;
CC -!- TISSUE SPECIFICITY: Expressed in larval and adult epidermis, intestine
CC and pharynx (PubMed:26371552). Broadly expressed in the nervous system
CC (PubMed:24569480, PubMed:26371552). Expressed in body wall muscle cells
CC (PubMed:24569477). {ECO:0000269|PubMed:24569477,
CC ECO:0000269|PubMed:24569480, ECO:0000269|PubMed:26371552}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development
CC (PubMed:24569477). Expressed in stretches and puncta in the body
CC syncytium and in puncta within seam cells (PubMed:26371552).
CC {ECO:0000269|PubMed:24569477, ECO:0000269|PubMed:26371552}.
CC -!- DOMAIN: The CKK domain binds microtubules. Might be required for
CC microtubule stabilization (PubMed:27661253). {ECO:0000255|PROSITE-
CC ProRule:PRU00841, ECO:0000269|PubMed:27661253}.
CC -!- DOMAIN: The Calponin-homology (CH) domain might negatively regulate the
CC CKK domain. {ECO:0000269|PubMed:27661253}.
CC -!- DOMAIN: The coiled-coil domain contributes to microtubule binding and
CC might negatively regulate the CKK domain.
CC {ECO:0000269|PubMed:27661253}.
CC -!- DISRUPTION PHENOTYPE: Viable with no gross morphological defects, but
CC exhibit uncoordinated locomotion and body positioning (PubMed:24569477,
CC PubMed:24569480, PubMed:26371552). Small reduction in the density of
CC microtubule bundles along the length of the body (PubMed:25437544,
CC PubMed:26371552). Fewer microtubules in the axons of PLM and ALM
CC neurons (PubMed:25437544, PubMed:24569477). Defective touch neuron
CC morphology with ectopic neurites extending from the cell bodies of ALM
CC neurons (PubMed:25437544). Irregular PLM neuron morphology including
CC defective PLM neuron commissure extension, loss of collateral branches,
CC presynaptic varicosities, overextended neurites and abnormal synapse
CC localization as identified by lack of small GTPase rab-3 and snb-1 at
CC synaptic patches (PubMed:24569477, PubMed:24569480). Impaired PLM
CC neuron regeneration following severing of the PLM axon
CC (PubMed:25437544). Loss of circumferential microtubule bundles and
CC shortening of remaining bundles (PubMed:27661253). Increased
CC microtubule growth rates (PubMed:27661253). Delayed wound closure
CC (PubMed:27661253). Treatment with a microtubule stabilizing drug,
CC paclitaxel, results in epidermal morphology defects (PubMed:27661253).
CC Treatment with a microtubule destabilizing drug, colchicine, results in
CC loss of light touch sensitivity and ectopic sprouting from neuronal
CC axons (PubMed:24569477). Double knockout with noca-1 isoforms results
CC in severe developmental defects with 60% not surviving beyond early
CC postembryonic stages, mainly dying at the larval developmental stage
CC L4, and slow growth with surviving mutants being smaller in size and
CC uncoordinated (PubMed:26371552). Double mutants also have significantly
CC fewer microtubule bundles along the length of the body, broken or
CC branched seam cell syncytia that is disconnected from the head and the
CC cuticles have increased permeability (PubMed:26371552). In a dapk-1
CC mutant background, suppression of the epidermal morphology defects
CC (PubMed:27661253). {ECO:0000269|PubMed:24569477,
CC ECO:0000269|PubMed:24569480, ECO:0000269|PubMed:25437544,
CC ECO:0000269|PubMed:26371552, ECO:0000269|PubMed:27661253}.
CC -!- SIMILARITY: Belongs to the CAMSAP1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00841}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BX284606; CDH92934.1; -; Genomic_DNA.
DR EMBL; BX284606; CCD66253.2; -; Genomic_DNA.
DR EMBL; BX284606; CDH92935.1; -; Genomic_DNA.
DR EMBL; BX284606; CDM63458.1; -; Genomic_DNA.
DR RefSeq; NP_001294829.1; NM_001307900.1. [U4PAZ9-4]
DR RefSeq; NP_001294846.1; NM_001307917.1. [U4PAZ9-1]
DR RefSeq; NP_001294847.1; NM_001307918.1. [U4PAZ9-3]
DR RefSeq; NP_510751.4; NM_078350.6. [U4PAZ9-2]
DR AlphaFoldDB; U4PAZ9; -.
DR IntAct; U4PAZ9; 1.
DR STRING; 6239.F35B3.5c; -.
DR PaxDb; U4PAZ9; -.
DR EnsemblMetazoa; F35B3.5a.1; F35B3.5a.1; WBGene00004121. [U4PAZ9-2]
DR EnsemblMetazoa; F35B3.5c.1; F35B3.5c.1; WBGene00004121. [U4PAZ9-1]
DR EnsemblMetazoa; F35B3.5d.1; F35B3.5d.1; WBGene00004121. [U4PAZ9-3]
DR EnsemblMetazoa; F35B3.5e.1; F35B3.5e.1; WBGene00004121. [U4PAZ9-4]
DR GeneID; 181743; -.
DR KEGG; cel:CELE_F35B3.5; -.
DR UCSC; F35B3.5a; c. elegans.
DR CTD; 181743; -.
DR WormBase; F35B3.5a; CE48430; WBGene00004121; ptrn-1. [U4PAZ9-2]
DR WormBase; F35B3.5c; CE48765; WBGene00004121; ptrn-1. [U4PAZ9-1]
DR WormBase; F35B3.5d; CE48517; WBGene00004121; ptrn-1. [U4PAZ9-3]
DR WormBase; F35B3.5e; CE49594; WBGene00004121; ptrn-1. [U4PAZ9-4]
DR eggNOG; KOG3654; Eukaryota.
DR GeneTree; ENSGT00950000182975; -.
DR HOGENOM; CLU_274207_0_0_1; -.
DR OMA; KESVPHI; -.
DR OrthoDB; 162094at2759; -.
DR PRO; PR:U4PAZ9; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00004121; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0036449; C:microtubule minus-end; IDA:WormBase.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
DR GO; GO:0005516; F:calmodulin binding; IEA:InterPro.
DR GO; GO:0051011; F:microtubule minus-end binding; IDA:WormBase.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IGI:WormBase.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; IBA:GO_Central.
DR GO; GO:0002119; P:nematode larval development; IGI:WormBase.
DR Gene3D; 1.10.418.10; -; 1.
DR Gene3D; 3.10.20.360; -; 1.
DR InterPro; IPR032940; CAMSAP.
DR InterPro; IPR022613; CAMSAP-like_CH_dom.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR038209; CKK_dom_sf.
DR InterPro; IPR014797; CKK_domain.
DR InterPro; IPR011033; PRC_barrel-like_sf.
DR PANTHER; PTHR21595; PTHR21595; 2.
DR Pfam; PF11971; CAMSAP_CH; 1.
DR Pfam; PF08683; CAMSAP_CKK; 1.
DR SMART; SM01051; CAMSAP_CKK; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR SUPFAM; SSF50346; SSF50346; 1.
DR PROSITE; PS50021; CH; 1.
DR PROSITE; PS51508; CKK; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cell projection; Coiled coil;
KW Cytoplasm; Cytoskeleton; Membrane; Microtubule; Reference proteome.
FT CHAIN 1..1112
FT /note="Patronin (microtubule-binding protein) homolog"
FT /evidence="ECO:0000305"
FT /id="PRO_0000436173"
FT DOMAIN 165..286
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 972..1109
FT /note="CKK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00841"
FT REGION 324..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 542..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 788..834
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 916..965
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 850..914
FT /evidence="ECO:0000255"
FT COMPBIAS 344..358
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 800..834
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 922..965
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..726
FT /note="Missing (in isoform d)"
FT /evidence="ECO:0000305"
FT /id="VSP_058271"
FT VAR_SEQ 1..515
FT /note="Missing (in isoform e)"
FT /evidence="ECO:0000305"
FT /id="VSP_058272"
FT VAR_SEQ 431..432
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_058273"
SQ SEQUENCE 1112 AA; 125606 MW; 721FB39A3BB9CBD5 CRC64;
MDFPLPALLA IEDYDENEGK LAASIRWLIS RVYEEKRDMP DKLRDGVQRD ENGHFQIDEA
VVGALCNGSL YAQAAAKIFK ESALVTKGHG AVLAVLTDYG IDVLHDGNEL VEEAQLVASA
PFNMSAHLAI IDALMMAHLR DVIPVSRVVE AVSRHTAVEP SEKPIDSVDA LLFWINKICL
LVRDDVERED SNTNIPEMED LYEDISDGQC LCALLHWYRP HEMPVADISF NDSATTRDCQ
YNLMLLQLFC RHHLAVDPFH FEIEDLLYLR DSLQMNVNAF LADLFVQFEP PVTPEPVETP
RIGPSPRRFV PASAIPDLRA ANAAARSSMH NRNRPRMYNP PPAVSHSQGP SRSVSRMSQD
SLFYSRPASI ALQRRSMDQD SVTDFQTIRQ GFENQAGTAQ LNRYDGSVTA SVRLAMEEKR
RKHDQQMAQM SFSSANETER LEKSKAAFFA LRKNDNDQTS KGKEEWYDHF EAKLRALELR
VGLEEGEDGT QSARLNRASS QPSVVQAGQT YPANYMTLPM NAAAQMTQSY IQHPQTPHDY
YMQQQMQQQQ QQQAQAQSNY ASPSQLRNSL SNGMINHAGY IVQSMYPGDY QQQQQQMQMQ
QGQMPVQPVG AYTPEGYFIP HHMQPIPVQQ GYQQMPQPGM GFNGMPATSQ PGFNMEGSPA
QMGYIQTANK PLDMEMPMQQ QPPQQPPQQM LPPNQNAFHL HSKSDDATQV QADPPLEINR
NLTNWGMTYK QEMPARSIPS RRTWQNETFI KNELDLVNSK ESVPHITDET TTQPEEAARR
FPDLMLDNHS ENLAPGRGFS RQNDRDDLST GRKSDDSPTD TPGRTFDDDE GSGENMEKIA
NERRIAKKAA LIAKTMKRKE EIETKVDLAE QRNAERRQVE NEKKELALRK KVEKEQQRQK
ILDEYKRKKL EKELGAELSA RSTGRGHSQP PFIRTKSQMS EVTESSRQNT PRMRGQSSVE
QRVSVSSLAE PTHKLYAKTV TKSNRGLINN ALQFSVFPGA VNNATRQATI TQMASSSSKH
FLILFRDQKC QYRGLYTWDE ISDTAVKISG QGPPKCTEAM MNSMFKYDSG AKNFTNIATK
HLSATIDGFA ILDQYWQKAR IPHSGTPAHK NN
