Reviewed, UniProtKB/Swiss-Prot P13796 (PLSL_HUMAN)

Names and origin

Protein names

Recommended name:
    Plastin-2
Alternative name(s):
    L-plastin
    Lymphocyte cytosolic protein 1
      Short name=LCP-1
    LC64P

Gene names

Name:	LCP1
Synonyms:	PLS2

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	627 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Actin-binding protein. Plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. Modulates the cell surface expression of IL2RA/CD25 and CD69. Ref.11 Ref.13
Subunit structure	Monomer. Interacts with AIF1 By similarity.
Subcellular location	Cytoplasm › cytoskeleton. Cell junction. Cell projection. Cell projection › ruffle membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Note: Relocalizes to the immunological synapse between peripheral blood T lymphocytes and antibody-presenting cells in response to costimulation through TCR/CD3 and CD2 or CD28. Associated with the actin cytoskeleton at membrane ruffles By similarity. Relocalizes to actin-rich cell projections upon serine phosphorylation.
Tissue specificity	Detected in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia, in spleen and other lymph node-containing organs. Expressed in peripheral blood T lymphocytes, neutrophils, monocytes, B lymphocytes, and myeloid cells. Ref.9
Post-translational modification	Phosphorylated on a serine residue in response to costimulation through TCR/CD3 and CD2 or CD28. Serine phosphorylation promotes association with the actin cytoskeleton and targeting to peripheral cell projections. Ref.11 Ref.13 Ref.10 Ref.12 Ref.14 The N-terminus is blocked.
Sequence similarities	Contains 2 actin-binding domains. Contains 4 CH (calponin-homology) domains. Contains 2 EF-hand domains.

Ontologies

Keywords
Cellular component	Cell junction Cell membrane Cell projection Cytoplasm Cytoskeleton Membrane
Coding sequence diversity	Polymorphism
Domain	Repeat
Ligand	Actin-binding Calcium
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	T cell activation during immune response Ref.13 Inferred from direct assay. Source: UniProtKB regulation of intracellular protein transport Ref.13 Inferred from direct assay. Source: UniProtKB
Cellular component	cytosol Ref.8 Ref.13 Inferred from direct assay. Source: UniProtKB
Molecular function	calcium ion binding Ref.2 Non-traceable author statement. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ATXN2	Q99700	1	EBI-698036,EBI-697691

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.6

Chain

2 – 627

626

Plastin-2

PRO_0000073743

Regions

Domain

9 – 44

36

EF-hand 1

Domain

49 – 84

36

EF-hand 2

Domain

106 – 379

274

Actin-binding 1

Domain

120 – 236

117

CH 1

Domain

264 – 375

112

CH 2

Domain

380 – 624

245

Actin-binding 2

Domain

394 – 503

110

CH 3

Domain

515 – 624

110

CH 4

Calcium binding

22 – 33

12

1 By similarity

Calcium binding

62 – 73

12

2 By similarity

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.6

Modified residue

5

1

Phosphoserine Ref.11 Ref.13 Ref.14

Modified residue

7

1

Phosphoserine By similarity

Modified residue

28

1

Phosphotyrosine Ref.12

Modified residue

76

1

N6-acetyllysine Ref.16

Modified residue

88

1

N6-acetyllysine Ref.16

Modified residue

124

1

Phosphotyrosine Ref.10

Modified residue

276

1

Phosphotyrosine Ref.12

Modified residue

294

1

N6-acetyllysine Ref.16

Modified residue

297

1

N6-acetyllysine Ref.16

Modified residue

361

1

N6-acetyllysine Ref.16

Modified residue

472

1

N6-acetyllysine Ref.16

Modified residue

542

1

N6-acetyllysine Ref.16

Modified residue

579

1

N6-acetyllysine Ref.16

Natural variations

Natural variant

24

1

D → E

VAR_001371

Natural variant

533

1

E → K: dbSNP rs4941543.

VAR_024398

Natural variant

544

1

P → A: dbSNP rs17067725.

VAR_030826

Experimental info

Mutagenesis

5

1

S → A: Abolishes phosphorylation and reduces the cell surface expression of CD69 and IL2RA. Reduces association with the actin cytoskeleton. Ref.11 Ref.13

Mutagenesis

5

1

S → E: Promotes association with the actin cytoskeleton. Ref.11 Ref.13

Sequence conflict

611

1

M → T AA sequence Ref.9

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

627

Helix Strand Turn

Details...

Helix

520 – 532

13

Helix

545 – 548

4

Helix

550 – 559

10

Turn

566 – 568

3

Helix

576 – 592

17

Helix

601 – 604

4

Turn

605 – 607

3

Helix

609 – 612

4

Helix

615 – 619

5

Sequences

	Sequence		Length	Mass (Da)
	P13796-1 [UniParc]. Last modified January 23, 2007. Version 5. Checksum: 6E2CC08E09DC75B6	FASTA	627	70,289
	10 20 30 40 50 60 MARGSVSDEE MMELREAFAK VDTDGNGYIS FNELNDLFKA ACLPLPGYRV REITENLMAT 70 80 90 100 110 120 GDLDQDGRIS FDEFIKIFHG LKSTDVAKTF RKAINKKEGI CAIGGTSEQS SVGTQHSYSE 130 140 150 160 170 180 EEKYAFVNWI NKALENDPDC RHVIPMNPNT NDLFNAVGDG IVLCKMINLS VPDTIDERTI 190 200 210 220 230 240 NKKKLTPFTI QENLNLALNS ASAIGCHVVN IGAEDLKEGK PYLVLGLLWQ VIKIGLFADI 250 260 270 280 290 300 ELSRNEALIA LLREGESLED LMKLSPEELL LRWANYHLEN AGCNKIGNFS TDIKDSKAYY 310 320 330 340 350 360 HLLEQVAPKG DEEGVPAVVI DMSGLREKDD IQRAECMLQQ AERLGCRQFV TATDVVRGNP 370 380 390 400 410 420 KLNLAFIANL FNRYPALHKP ENQDIDWGAL EGETREERTF RNWMNSLGVN PRVNHLYSDL 430 440 450 460 470 480 SDALVIFQLY EKIKVPVDWN RVNKPPYPKL GGNMKKLENC NYAVELGKNQ AKFSLVGIGG 490 500 510 520 530 540 QDLNEGNRTL TLALIWQLMR RYTLNILEEI GGGQKVNDDI IVNWVNETLR EAEKSSSISS 550 560 570 580 590 600 FKDPKISTSL PVLDLIDAIQ PGSINYDLLK TENLNDDEKL NNAKYAISMA RKIGARVYAL 610 620 PEDLVEVNPK MVMTVFACLM GKGMKRV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and characterization of plastin, a human leukocyte protein expressed in transformed human fibroblasts." Lin C.-S., Aebersold R.H., Kent S.B., Varma M., Leavitt J. Mol. Cell. Biol. 8:4659-4668(1988) [PubMed: 3211125] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 58-627, PARTIAL PROTEIN SEQUENCE.
[2]	"Correction of the N-terminal sequences of the human plastin isoforms by using anchored polymerase chain reaction: identification of a potential calcium-binding domain." Lin C.-S., Aebersold R.H., Leavitt J. Mol. Cell. Biol. 10:1818-1821(1990) [PubMed: 2378651] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-140, SEQUENCE REVISION.
[3]	"65-kilodalton protein phosphorylated by interleukin 2 stimulation bears two putative actin-binding sites and two calcium-binding sites." Zu Y., Shigesada K., Nishida E., Kubota I., Kohno M., Hanaoka M., Namba Y. Biochemistry 29:8319-8324(1990) [PubMed: 2252891] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Amygdala.
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lymph and Placenta.
[6]	Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M. Submitted (MAY-2006) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-14; 20-31; 184-192 AND 534-541, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY. Tissue: T-cell.
[7]	"Human plastin genes. Comparative gene structure, chromosome location, and differential expression in normal and neoplastic cells." Lin C.-S., Park T., Chen Z.P., Leavitt J. J. Biol. Chem. 268:2781-2792(1993) [PubMed: 8428952] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 585-627.
[8]	"Characterization of interleukin 2 stimulated 65-kilodalton phosphoprotein in human T cells." Zu Y., Kohno M., Kubota I., Nishida E., Hanaoka M., Namba Y. Biochemistry 29:1055-1062(1990) [PubMed: 2111166] [Abstract] Cited for: PROTEIN SEQUENCE OF 264-283; 517-533 AND 593-609.
[9]	"Purification and characterization of a cytosolic 65-kilodalton phosphoprotein in human leukocytes whose phosphorylation is augmented by stimulation with interleukin 1." Matsushima K., Shiroo M., Kung H.F., Copeland T.D. Biochemistry 27:3765-3770(1988) [PubMed: 3261603] [Abstract] Cited for: PROTEIN SEQUENCE OF 590-611, TISSUE SPECIFICITY.
[10]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-124, MASS SPECTROMETRY.
[11]	"Phosphorylation on Ser5 increases the F-actin-binding activity of L-plastin and promotes its targeting to sites of actin assembly in cells." Janji B., Giganti A., De Corte V., Catillon M., Bruyneel E., Lentz D., Plastino J., Gettemans J., Friederich E. J. Cell Sci. 119:1947-1960(2006) [PubMed: 16636079] [Abstract] Cited for: FUNCTION, ACTIN-BINDING, INTERACTION WITH ACTIN FIBERS, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-5, PHOSPHORYLATION AT SER-5.
[12]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-28 AND TYR-276, MASS SPECTROMETRY.
[13]	"Costimulation induced phosphorylation of L-plastin facilitates surface transport of the T cell activation molecules CD69 and CD25." Wabnitz G.H., Koecher T., Lohneis P., Stober C., Konstandin M.H., Funk B., Sester U., Wilm M., Klemke M., Samstag Y. Eur. J. Immunol. 37:649-662(2007) [PubMed: 17294403] [Abstract] Cited for: SUBCELLULAR LOCATION, FUNCTION, MUTAGENESIS OF SER-5, PHOSPHORYLATION AT SER-5, MASS SPECTROMETRY.
[14]	"Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment." Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J. J. Proteome Res. 7:5167-5176(2008) [PubMed: 19367720] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5, MASS SPECTROMETRY. Tissue: T-cell.
[15]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[16]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-76; LYS-88; LYS-294; LYS-297; LYS-361; LYS-472; LYS-542 AND LYS-579, MASS SPECTROMETRY.
[17]	"Solution structure of the fourth CH domain from human L-plastin." RIKEN structural genomics initiative (RSGI) Submitted (JUN-2006) to the PDB data bank Cited for: STRUCTURE BY NMR OF 513-627.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBLGenBankDDBJ

M22300 mRNA. Translation: AAB02845.1.
M34426 mRNA. Translation: AAA36184.1.
J02923 mRNA. Translation: AAA63236.1.
AK312393 mRNA. Translation: BAG35310.1.
BC007673 mRNA. Translation: AAH07673.1.
BC010271 mRNA. Translation: AAH10271.1.
L05492 Genomic DNA. Translation: AAA59529.1.

IPI

IPI00010471.

PIR

A35836.

RefSeq

NP_002289.2.

UniGene

Hs.381099
Hs.710563

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2D85	NMR	-	A	517-627	[»]

SMR

P13796. Positions 117-371, 118-372.

ModBase

Search...

Protein-protein interaction databases

IntAct

P13796. 1 interaction.

STRING

P13796.

PTM databases

PhosphoSite

P13796.

Proteomic databases

PRIDE

P13796.

Genome annotation databases

Ensembl

ENST00000323076; ENSP00000315757; ENSG00000136167; Homo sapiens. [Genome view]
ENST00000398576; ENSP00000381581; ENSG00000136167; Homo sapiens. [Genome view]
ENST00000416500; ENSP00000408052; ENSG00000136167; Homo sapiens. [Genome view]
ENST00000435666; ENSP00000405134; ENSG00000136167; Homo sapiens. [Genome view]
ENST00000442275; ENSP00000402157; ENSG00000136167; Homo sapiens. [Genome view]
ENST00000450064; ENSP00000407907; ENSG00000136167; Homo sapiens. [Genome view]

GeneID

3936.

KEGG

hsa:3936.

Organism-specific databases

CTD

3936.

GeneCards

GC13M045598.

HGNC

HGNC:6528. LCP1.

HPA

CAB020673.
HPA019493.

MIM

153430. gene.

PharmGKB

PA134924593.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P13796.

HOVERGEN

P13796.

Gene expression databases

ArrayExpress

P13796.

Bgee

P13796.

CleanEx

HS_LCP1.

Genevestigator

P13796.

GermOnline

ENSG00000136167. Homo sapiens.

Family and domain databases

InterPro

IPR001589. Actinin_actin-bd_CS.
IPR001715. Calponin_act_bd.
IPR011992. EF-Hand_type.
IPR018248. EF_hand.
IPR018247. EF_HAND_1_Ca_BS.
IPR018249. EF_HAND_2.
IPR002048. EF_hand_Ca_bd.
[Graphical view]

Gene3D

G3DSA:1.10.418.10. Calponin-homology. 4 hits.
G3DSA:1.10.238.10. EF-Hand_type. 1 hit.

Pfam

PF00307. CH. 4 hits.
PF00036. efhand. 2 hits.
[Graphical view]

ProDom

PD000012. EF-hand. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00033. CH. 4 hits.
SM00054. EFh. 2 hits.
[Graphical view]

PROSITE

PS00019. ACTININ_1. 2 hits.
PS00020. ACTININ_2. 2 hits.
PS50021. CH. 4 hits.
PS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 2 hits.
[Graphical view]

ProtoNet

Search...

Other Resources

SOURCE

Search...

Entry information

Entry name

PLSL_HUMAN

Accession

Primary (citable) accession number: P13796
Secondary accession number(s): B2R613

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	January 23, 2007
Last modified:	November 3, 2009
This is version 124 of the entry and version 5 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.