PALLD_RAT
ID PALLD_RAT Reviewed; 603 AA.
AC P0C5E3;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Palladin;
DE Flags: Fragment;
GN Name=Palld;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP FUNCTION.
RX PubMed=10931874; DOI=10.1083/jcb.150.3.643;
RA Parast M.M., Otey C.A.;
RT "Characterization of palladin, a novel protein localized to stress fibers
RT and cell adhesions.";
RL J. Cell Biol. 150:643-656(2000).
RN [3]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=11438925; DOI=10.1002/cne.1062.abs;
RA Hwang S.J., Pagliardini S., Boukhelifa M., Parast M.M., Otey C.A.,
RA Rustioni A., Valtschanoff J.G.;
RT "Palladin is expressed preferentially in excitatory terminals in the rat
RT central nervous system.";
RL J. Comp. Neurol. 436:211-224(2001).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=11553711; DOI=10.1091/mbc.12.9.2721;
RA Boukhelifa M., Parast M.M., Valtschanoff J.G., LaMantia A.S., Meeker R.B.,
RA Otey C.A.;
RT "A role for the cytoskeleton-associated protein palladin in neurite
RT outgrowth.";
RL Mol. Biol. Cell 12:2721-2729(2001).
RN [5]
RP FUNCTION, AND INDUCTION.
RX PubMed=12932445; DOI=10.1016/s1044-7431(03)00127-1;
RA Boukhelifa M., Hwang S.J., Valtschanoff J.G., Meeker R.B., Rustioni A.,
RA Otey C.A.;
RT "A critical role for palladin in astrocyte morphology and response to
RT injury.";
RL Mol. Cell. Neurosci. 23:661-668(2003).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=16125169; DOI=10.1016/j.yexcr.2005.06.026;
RA Roenty M., Taivainen A., Moza M., Kruh G.D., Ehler E., Carpen O.;
RT "Involvement of palladin and alpha-actinin in targeting of the Abl/Arg
RT kinase adaptor ArgBP2 to the actin cytoskeleton.";
RL Exp. Cell Res. 310:88-98(2005).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=16868024; DOI=10.1242/jcs.03076;
RA Goicoechea S., Arneman D., Disanza A., Garcia-Mata R., Scita G., Otey C.A.;
RT "Palladin binds to Eps8 and enhances the formation of dorsal ruffles and
RT podosomes in vascular smooth muscle cells.";
RL J. Cell Sci. 119:3316-3324(2006).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=22659164; DOI=10.1016/j.yexcr.2012.05.006;
RA Miyazaki K., Ohno K., Tamura N., Sasaki T., Sato K.;
RT "CLP36 and RIL recruit alpha-actinin-1 to stress fibers and differentially
RT regulate stress fiber dynamics in F2408 fibroblasts.";
RL Exp. Cell Res. 318:1716-1725(2012).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133; SER-170; SER-393 AND
RP SER-398, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [10]
RP INTERACTION WITH RAI14.
RX PubMed=23565266; DOI=10.1371/journal.pone.0060656;
RA Qian X., Mruk D.D., Cheng C.Y.;
RT "Rai14 (retinoic acid induced protein 14) is involved in regulating f-actin
RT dynamics at the ectoplasmic specialization in the rat testis.";
RL PLoS ONE 8:E60656-E60656(2013).
CC -!- FUNCTION: Cytoskeletal protein required for organization of normal
CC actin cytoskeleton. Roles in establishing cell morphology, motility,
CC cell adhesion and cell-extracellular matrix interactions in a variety
CC of cell types. May function as a scaffolding molecule with the
CC potential to influence both actin polymerization and the assembly of
CC existing actin filaments into higher-order arrays. Binds to proteins
CC that bind to either monomeric or filamentous actin. Localizes at sites
CC where active actin remodeling takes place, such as lamellipodia and
CC membrane ruffles. Different isoforms may have functional differences.
CC Plays a role in neurite outgrowth and in the establishment of polarity
CC during neuronal morphogenesis. Participates in the acquisition of the
CC reactive astrocyte morphology. {ECO:0000269|PubMed:10931874,
CC ECO:0000269|PubMed:11553711, ECO:0000269|PubMed:12932445,
CC ECO:0000269|PubMed:16868024}.
CC -!- SUBUNIT: Interacts with EPS8 (By similarity). Interacts with LASP1 (By
CC similarity). Interacts with VASP (By similarity). Interacts with ACTN
CC (By similarity). Interacts with SORBS2 (By similarity). Interacts with
CC PFN1 (By similarity). Interacts with LPP (By similarity). Interacts
CC with SPIN90 (By similarity). Interacts with SRC (By similarity).
CC Interacts with EZR (By similarity). Interacts with RAI14
CC (PubMed:23565266). {ECO:0000250|UniProtKB:Q8WX93,
CC ECO:0000250|UniProtKB:Q9ET54, ECO:0000269|PubMed:23565266}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:16125169, ECO:0000269|PubMed:16868024}. Cell
CC junction, focal adhesion {ECO:0000250|UniProtKB:Q8WX93}. Cytoplasm,
CC myofibril, sarcomere, Z line {ECO:0000269|PubMed:11553711,
CC ECO:0000269|PubMed:16125169}. Cell projection, ruffle
CC {ECO:0000269|PubMed:16868024}. Cell projection, podosome
CC {ECO:0000269|PubMed:16868024}. Cell projection, lamellipodium
CC {ECO:0000250|UniProtKB:Q8WX93}. Cell projection, axon
CC {ECO:0000269|PubMed:11438925, ECO:0000269|PubMed:11553711}. Cell
CC projection, growth cone {ECO:0000269|PubMed:11438925,
CC ECO:0000269|PubMed:11553711}. Note=Localizes to stress fibers
CC (PubMed:16868024, PubMed:11553711, PubMed:16125169, PubMed:22659164).
CC Localizes to Z lines (PubMed:16868024, PubMed:11553711,
CC PubMed:16125169). Preferentially expressed in the excitatory
CC presynaptic terminals (PubMed:11438925). {ECO:0000269|PubMed:11438925,
CC ECO:0000269|PubMed:11553711, ECO:0000269|PubMed:16125169,
CC ECO:0000269|PubMed:16868024, ECO:0000269|PubMed:22659164}.
CC -!- TISSUE SPECIFICITY: In adult central nervous system is detected in the
CC brain and spinal cord, specially in the olfactory bulb, cerebral and
CC cerebellar cortices, hippocampus, amygdala, superior colluculus, and
CC superficial laminae of the spinal dorsal horn.
CC {ECO:0000269|PubMed:11438925}.
CC -!- DEVELOPMENTAL STAGE: Early expressed in the axonal compartment in
CC developing neurons, and persists in this polarized distribution in the
CC adult brain. {ECO:0000269|PubMed:11553711}.
CC -!- INDUCTION: Up-regulated rapidly and persistently in astrocytes in
CC response to injury. {ECO:0000269|PubMed:12932445,
CC ECO:0000269|PubMed:16868024}.
CC -!- PTM: Phosphorylated predominantly on serines and, to a lesser extent,
CC on tyrosines. Phosphorylation at Ser-395 by PKB/AKT1 modulates
CC cytoskeletal organization and cell motility (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the myotilin/palladin family. {ECO:0000305}.
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; AC080188; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC084353; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC115538; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P0C5E3; -.
DR SMR; P0C5E3; -.
DR STRING; 10116.ENSRNOP00000059489; -.
DR iPTMnet; P0C5E3; -.
DR PhosphoSitePlus; P0C5E3; -.
DR PeptideAtlas; P0C5E3; -.
DR PRIDE; P0C5E3; -.
DR RGD; 2322545; Palld.
DR eggNOG; ENOG502QSRV; Eukaryota.
DR InParanoid; P0C5E3; -.
DR PhylomeDB; P0C5E3; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005884; C:actin filament; ISO:RGD.
DR GO; GO:0030424; C:axon; IDA:UniProtKB.
DR GO; GO:0044295; C:axonal growth cone; IDA:RGD.
DR GO; GO:0005856; C:cytoskeleton; IDA:UniProtKB.
DR GO; GO:0060076; C:excitatory synapse; IDA:UniProtKB.
DR GO; GO:0030175; C:filopodium; IDA:RGD.
DR GO; GO:0005925; C:focal adhesion; ISO:RGD.
DR GO; GO:0030426; C:growth cone; IDA:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0002102; C:podosome; IDA:RGD.
DR GO; GO:0001726; C:ruffle; IDA:RGD.
DR GO; GO:0001725; C:stress fiber; IDA:UniProtKB.
DR GO; GO:0030018; C:Z disc; IDA:UniProtKB.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0098632; F:cell-cell adhesion mediator activity; IBA:GO_Central.
DR GO; GO:0008092; F:cytoskeletal protein binding; IPI:RGD.
DR GO; GO:0030036; P:actin cytoskeleton organization; ISO:RGD.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; IEA:InterPro.
DR GO; GO:0071456; P:cellular response to hypoxia; IEP:RGD.
DR GO; GO:0070593; P:dendrite self-avoidance; IBA:GO_Central.
DR GO; GO:0003382; P:epithelial cell morphogenesis; ISO:RGD.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IBA:GO_Central.
DR GO; GO:0003334; P:keratinocyte development; ISO:RGD.
DR GO; GO:0031175; P:neuron projection development; IMP:RGD.
DR GO; GO:0071803; P:positive regulation of podosome assembly; IMP:RGD.
DR GO; GO:0031529; P:ruffle organization; IMP:RGD.
DR GO; GO:0060707; P:trophoblast giant cell differentiation; IEP:RGD.
DR GO; GO:0042060; P:wound healing; IEP:RGD.
DR CDD; cd05893; Ig_Palladin_C; 1.
DR Gene3D; 2.60.40.10; -; 4.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR033017; Palladin_C.
DR Pfam; PF07679; I-set; 3.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 3.
DR SUPFAM; SSF48726; SSF48726; 4.
DR PROSITE; PS50835; IG_LIKE; 3.
PE 1: Evidence at protein level;
KW Actin-binding; Cell junction; Cell projection; Cytoplasm; Cytoskeleton;
KW Disulfide bond; Immunoglobulin domain; Phosphoprotein; Reference proteome;
KW Repeat.
FT CHAIN <1..>603
FT /note="Palladin"
FT /id="PRO_0000302722"
FT DOMAIN 278..362
FT /note="Ig-like C2-type 1"
FT DOMAIN 412..503
FT /note="Ig-like C2-type 2"
FT DOMAIN 511..601
FT /note="Ig-like C2-type 3"
FT REGION 63..67
FT /note="Interaction with VASP"
FT /evidence="ECO:0000250"
FT REGION 134..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 373..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 414..503
FT /note="Interaction with EZR"
FT /evidence="ECO:0000250"
FT REGION 513..603
FT /note="Interaction with EZR"
FT /evidence="ECO:0000250"
FT COMPBIAS 140..154
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 136
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9ET54"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WX93"
FT MOD_RES 170
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 256
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WX93"
FT MOD_RES 261
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WX93"
FT MOD_RES 378
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WX93"
FT MOD_RES 381
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WX93"
FT MOD_RES 393
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 395
FT /note="Phosphoserine; by PKB/AKT1"
FT /evidence="ECO:0000250|UniProtKB:Q8WX93"
FT MOD_RES 398
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT DISULFID 433..485
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT NON_TER 1
FT NON_TER 603
SQ SEQUENCE 603 AA; 66705 MW; 52B1D4277E77F05A CRC64;
PEEICTLVIA ESFPEDAGIF TCSARNDYGS VTSTAQLVVT SANTENCSYD SMGEPNSDHF
QHFPPPPPIL ETGSYELASQ KPSEIQQVNT PNLGFNMAAL QMQFNSAERE TNGVHPSHGV
NGLINGKAYG NKSPPTPAAL LSPTKEPPPL LAKPKLGFPK KASRTARIAS DEEIQGTKDA
VIQDLERKLR FKEDLLNNGQ PRLTYEERMA RRLLGADSAN VFNIQEPEET AANQEYKVSS
CEQRLISEIE YRLERSPVEE SGDEVQEAEV PVENAAAPFF EMKLKHYKIF EGMPVTFTCR
VAGSPKPKIY WFKDGKQISP KSDHYTIQRD VDGTCSLHTT ASTLDDDGNY TIMAANTQGR
VSCTGRLMVQ AVNQRGRSPR SPPGHPHARR PRSRSRDSGD ENEPIQERFF RPHFLQAPGD
LTVQEGKLCR MDCKVSGLPT PDLSWQLDGK PIRPDSAHKM LVRENGVHSL IIEPVTSRDA
GIYTCIATNR AGQNSFNLEL VVAAKEAHKA PVFIEKLQNT GVADGYPVRL ECRVSGVPPP
QIFWKKENES LTHSTDRVSM HQDNHGYICL LIQGATKEDA GWYTVSAKNE AGIVSCTARL
DVY
