Full text data of PLS1
PLS1
[Confidence: low (only semi-automatic identification from reviews)]
Plastin-1 (Intestine-specific plastin; I-plastin)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Plastin-1 (Intestine-specific plastin; I-plastin)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q14651
ID PLSI_HUMAN Reviewed; 629 AA.
AC Q14651; A8K2Q1; D3DNG3; Q8NEG6;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 03-MAR-2009, sequence version 2.
DT 22-JAN-2014, entry version 119.
DE RecName: Full=Plastin-1;
DE AltName: Full=Intestine-specific plastin;
DE Short=I-plastin;
GN Name=PLS1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Small intestine;
RX PubMed=8139549;
RA Lin C.-S., Shen W., Chen Z.P., Tu Y.-H., Matsudaira P.;
RT "Identification of I-plastin, a human fimbrin isoform expressed in
RT intestine and kidney.";
RL Mol. Cell. Biol. 14:2457-2467(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Actin-bundling protein in the absence of calcium.
CC -!- SUBUNIT: Monomer (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: In small intestine, colon, and kidney;
CC relatively lower levels of expression are detected in the lung and
CC stomach.
CC -!- PTM: Phosphorylated (By similarity).
CC -!- SIMILARITY: Contains 2 actin-binding domains.
CC -!- SIMILARITY: Contains 4 CH (calponin-homology) domains.
CC -!- SIMILARITY: Contains 2 EF-hand domains.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; L20826; AAA19869.1; -; mRNA.
DR EMBL; AK290316; BAF83005.1; -; mRNA.
DR EMBL; CH471052; EAW78965.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78967.1; -; Genomic_DNA.
DR EMBL; BC031083; AAH31083.1; -; mRNA.
DR PIR; A56536; A56536.
DR RefSeq; NP_001138791.1; NM_001145319.1.
DR RefSeq; NP_001165783.1; NM_001172312.1.
DR RefSeq; NP_002661.2; NM_002670.2.
DR UniGene; Hs.203637; -.
DR ProteinModelPortal; Q14651; -.
DR SMR; Q14651; 15-83, 120-628.
DR MINT; MINT-3029920; -.
DR STRING; 9606.ENSP00000336831; -.
DR PhosphoSite; Q14651; -.
DR DMDM; 224471848; -.
DR PaxDb; Q14651; -.
DR PRIDE; Q14651; -.
DR DNASU; 5357; -.
DR Ensembl; ENST00000337777; ENSP00000336831; ENSG00000120756.
DR Ensembl; ENST00000457734; ENSP00000387890; ENSG00000120756.
DR Ensembl; ENST00000497002; ENSP00000418700; ENSG00000120756.
DR GeneID; 5357; -.
DR KEGG; hsa:5357; -.
DR UCSC; uc003euz.3; human.
DR CTD; 5357; -.
DR GeneCards; GC03P142315; -.
DR H-InvDB; HIX0003743; -.
DR HGNC; HGNC:9090; PLS1.
DR HPA; HPA055744; -.
DR MIM; 602734; gene.
DR neXtProt; NX_Q14651; -.
DR PharmGKB; PA33417; -.
DR eggNOG; COG5069; -.
DR HOGENOM; HOG000213447; -.
DR HOVERGEN; HBG003082; -.
DR InParanoid; Q14651; -.
DR KO; K17275; -.
DR OMA; DDPDCKH; -.
DR OrthoDB; EOG7K9K2D; -.
DR PhylomeDB; Q14651; -.
DR GenomeRNAi; 5357; -.
DR NextBio; 20766; -.
DR PRO; PR:Q14651; -.
DR ArrayExpress; Q14651; -.
DR Bgee; Q14651; -.
DR CleanEx; HS_PLS1; -.
DR Genevestigator; Q14651; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0051015; F:actin filament binding; TAS:ProtInc.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:ProtInc.
DR Gene3D; 1.10.238.10; -; 1.
DR Gene3D; 1.10.418.10; -; 4.
DR InterPro; IPR001589; Actinin_actin-bd_CS.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR Pfam; PF00307; CH; 4.
DR Pfam; PF00036; EF-hand_1; 1.
DR Pfam; PF13405; EF-hand_6; 1.
DR SMART; SM00033; CH; 4.
DR SMART; SM00054; EFh; 2.
DR SUPFAM; SSF47576; SSF47576; 1.
DR PROSITE; PS00019; ACTININ_1; 2.
DR PROSITE; PS00020; ACTININ_2; 2.
DR PROSITE; PS50021; CH; 4.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; Calcium; Complete proteome; Cytoplasm;
KW Metal-binding; Phosphoprotein; Polymorphism; Reference proteome;
KW Repeat.
FT CHAIN 1 629 Plastin-1.
FT /FTId=PRO_0000073750.
FT DOMAIN 11 46 EF-hand 1.
FT DOMAIN 51 86 EF-hand 2.
FT DOMAIN 108 380 Actin-binding 1.
FT DOMAIN 122 238 CH 1.
FT DOMAIN 266 376 CH 2.
FT DOMAIN 381 625 Actin-binding 2.
FT DOMAIN 395 504 CH 3.
FT DOMAIN 516 625 CH 4.
FT CA_BIND 24 35 1 (Potential).
FT CA_BIND 64 75 2 (Potential).
FT MOD_RES 1 1 N-acetylmethionine.
FT VARIANT 146 146 I -> M (in dbSNP:rs35710125).
FT /FTId=VAR_048660.
FT VARIANT 216 216 S -> L (in dbSNP:rs35435507).
FT /FTId=VAR_048661.
FT CONFLICT 317 317 P -> L (in Ref. 2; BAF83005).
FT CONFLICT 441 441 S -> R (in Ref. 4; AAH31083).
FT CONFLICT 487 487 G -> R (in Ref. 1; AAA19869).
SQ SEQUENCE 629 AA; 70253 MW; F904031933C2C323 CRC64;
MENSTTTISR EELEELQEAF NKIDIDNSGY VSDYELQDLF KEASLPLPGY KVREIVEKIL
SVADSNKDGK ISFEEFVSLM QELKSKDISK TFRKIINKRE GITAIGGTST ISSEGTQHSY
SEEEKVAFVN WINKALENDP DCKHLIPMNP NDDSLFKSLA DGILLCKMIN LSEPDTIDER
AINKKKLTPF TISENLNLAL NSASAIGCTV VNIGASDLKE GKPHLVLGLL WQIIKVGLFA
DIEISRNEAL IALLNEGEEL EELMKLSPEE LLLRWVNYHL TNAGWHTISN FSQDIKDSRA
YFHLLNQIAP KGGEDGPAIA IDLSGINETN DLKRAGLMLQ EADKLGCKQF VTPADVVSGN
PKLNLAFVAN LFNTYPCLHK PNNNDIDMNL LEGESKEERT FRNWMNSLGV NPYINHLYSD
LADALVIFQL YEMIRVPVNW SHVNKPPYPA LGGNMKKIEN CNYAVELGKN KAKFSLVGIA
GQDLNEGNST LTLALVWQLM RRYTLNVLSD LGEGEKVNDE IIIKWVNQTL KSANKKTSIS
SFKDKSISTS LPVLDLIDAI APNAVRQEMI RRENLSDEDK LNNAKYAISV ARKIGARIYA
LPDDLVEVKP KMVMTVFACL MGKGLNRIK
//
ID PLSI_HUMAN Reviewed; 629 AA.
AC Q14651; A8K2Q1; D3DNG3; Q8NEG6;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 03-MAR-2009, sequence version 2.
DT 22-JAN-2014, entry version 119.
DE RecName: Full=Plastin-1;
DE AltName: Full=Intestine-specific plastin;
DE Short=I-plastin;
GN Name=PLS1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Small intestine;
RX PubMed=8139549;
RA Lin C.-S., Shen W., Chen Z.P., Tu Y.-H., Matsudaira P.;
RT "Identification of I-plastin, a human fimbrin isoform expressed in
RT intestine and kidney.";
RL Mol. Cell. Biol. 14:2457-2467(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Actin-bundling protein in the absence of calcium.
CC -!- SUBUNIT: Monomer (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: In small intestine, colon, and kidney;
CC relatively lower levels of expression are detected in the lung and
CC stomach.
CC -!- PTM: Phosphorylated (By similarity).
CC -!- SIMILARITY: Contains 2 actin-binding domains.
CC -!- SIMILARITY: Contains 4 CH (calponin-homology) domains.
CC -!- SIMILARITY: Contains 2 EF-hand domains.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; L20826; AAA19869.1; -; mRNA.
DR EMBL; AK290316; BAF83005.1; -; mRNA.
DR EMBL; CH471052; EAW78965.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78967.1; -; Genomic_DNA.
DR EMBL; BC031083; AAH31083.1; -; mRNA.
DR PIR; A56536; A56536.
DR RefSeq; NP_001138791.1; NM_001145319.1.
DR RefSeq; NP_001165783.1; NM_001172312.1.
DR RefSeq; NP_002661.2; NM_002670.2.
DR UniGene; Hs.203637; -.
DR ProteinModelPortal; Q14651; -.
DR SMR; Q14651; 15-83, 120-628.
DR MINT; MINT-3029920; -.
DR STRING; 9606.ENSP00000336831; -.
DR PhosphoSite; Q14651; -.
DR DMDM; 224471848; -.
DR PaxDb; Q14651; -.
DR PRIDE; Q14651; -.
DR DNASU; 5357; -.
DR Ensembl; ENST00000337777; ENSP00000336831; ENSG00000120756.
DR Ensembl; ENST00000457734; ENSP00000387890; ENSG00000120756.
DR Ensembl; ENST00000497002; ENSP00000418700; ENSG00000120756.
DR GeneID; 5357; -.
DR KEGG; hsa:5357; -.
DR UCSC; uc003euz.3; human.
DR CTD; 5357; -.
DR GeneCards; GC03P142315; -.
DR H-InvDB; HIX0003743; -.
DR HGNC; HGNC:9090; PLS1.
DR HPA; HPA055744; -.
DR MIM; 602734; gene.
DR neXtProt; NX_Q14651; -.
DR PharmGKB; PA33417; -.
DR eggNOG; COG5069; -.
DR HOGENOM; HOG000213447; -.
DR HOVERGEN; HBG003082; -.
DR InParanoid; Q14651; -.
DR KO; K17275; -.
DR OMA; DDPDCKH; -.
DR OrthoDB; EOG7K9K2D; -.
DR PhylomeDB; Q14651; -.
DR GenomeRNAi; 5357; -.
DR NextBio; 20766; -.
DR PRO; PR:Q14651; -.
DR ArrayExpress; Q14651; -.
DR Bgee; Q14651; -.
DR CleanEx; HS_PLS1; -.
DR Genevestigator; Q14651; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0051015; F:actin filament binding; TAS:ProtInc.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:ProtInc.
DR Gene3D; 1.10.238.10; -; 1.
DR Gene3D; 1.10.418.10; -; 4.
DR InterPro; IPR001589; Actinin_actin-bd_CS.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR Pfam; PF00307; CH; 4.
DR Pfam; PF00036; EF-hand_1; 1.
DR Pfam; PF13405; EF-hand_6; 1.
DR SMART; SM00033; CH; 4.
DR SMART; SM00054; EFh; 2.
DR SUPFAM; SSF47576; SSF47576; 1.
DR PROSITE; PS00019; ACTININ_1; 2.
DR PROSITE; PS00020; ACTININ_2; 2.
DR PROSITE; PS50021; CH; 4.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; Calcium; Complete proteome; Cytoplasm;
KW Metal-binding; Phosphoprotein; Polymorphism; Reference proteome;
KW Repeat.
FT CHAIN 1 629 Plastin-1.
FT /FTId=PRO_0000073750.
FT DOMAIN 11 46 EF-hand 1.
FT DOMAIN 51 86 EF-hand 2.
FT DOMAIN 108 380 Actin-binding 1.
FT DOMAIN 122 238 CH 1.
FT DOMAIN 266 376 CH 2.
FT DOMAIN 381 625 Actin-binding 2.
FT DOMAIN 395 504 CH 3.
FT DOMAIN 516 625 CH 4.
FT CA_BIND 24 35 1 (Potential).
FT CA_BIND 64 75 2 (Potential).
FT MOD_RES 1 1 N-acetylmethionine.
FT VARIANT 146 146 I -> M (in dbSNP:rs35710125).
FT /FTId=VAR_048660.
FT VARIANT 216 216 S -> L (in dbSNP:rs35435507).
FT /FTId=VAR_048661.
FT CONFLICT 317 317 P -> L (in Ref. 2; BAF83005).
FT CONFLICT 441 441 S -> R (in Ref. 4; AAH31083).
FT CONFLICT 487 487 G -> R (in Ref. 1; AAA19869).
SQ SEQUENCE 629 AA; 70253 MW; F904031933C2C323 CRC64;
MENSTTTISR EELEELQEAF NKIDIDNSGY VSDYELQDLF KEASLPLPGY KVREIVEKIL
SVADSNKDGK ISFEEFVSLM QELKSKDISK TFRKIINKRE GITAIGGTST ISSEGTQHSY
SEEEKVAFVN WINKALENDP DCKHLIPMNP NDDSLFKSLA DGILLCKMIN LSEPDTIDER
AINKKKLTPF TISENLNLAL NSASAIGCTV VNIGASDLKE GKPHLVLGLL WQIIKVGLFA
DIEISRNEAL IALLNEGEEL EELMKLSPEE LLLRWVNYHL TNAGWHTISN FSQDIKDSRA
YFHLLNQIAP KGGEDGPAIA IDLSGINETN DLKRAGLMLQ EADKLGCKQF VTPADVVSGN
PKLNLAFVAN LFNTYPCLHK PNNNDIDMNL LEGESKEERT FRNWMNSLGV NPYINHLYSD
LADALVIFQL YEMIRVPVNW SHVNKPPYPA LGGNMKKIEN CNYAVELGKN KAKFSLVGIA
GQDLNEGNST LTLALVWQLM RRYTLNVLSD LGEGEKVNDE IIIKWVNQTL KSANKKTSIS
SFKDKSISTS LPVLDLIDAI APNAVRQEMI RRENLSDEDK LNNAKYAISV ARKIGARIYA
LPDDLVEVKP KMVMTVFACL MGKGLNRIK
//
MIM
602734
*RECORD*
*FIELD* NO
602734
*FIELD* TI
*602734 PLASTIN 1; PLS1
;;INTESTINE-SPECIFIC PLASTIN;;
I-PLASTIN;;
FIMBRIN
*FIELD* TX
read more
CLONING
Fimbrin is an actin-bundling protein that was originally discovered in
chicken intestinal brush border microvilli. By screening a human small
intestine cDNA library with a chicken fimbrin cDNA, Lin et al. (1994)
identified a cDNA encoding I-plastin. Northern blot analysis revealed
that I-plastin was expressed as a 3.7-kb mRNA in human colon and small
intestine. A survey of rat tissues detected I-plastin expression
primarily in the intestine, with a lower level in the kidneys. By
immunofluorescence, Lin et al. (1994) localized I-plastin to the brush
border of the human small intestine and colon. The predicted 629-amino
acid protein is 86%, 75%, and 73% identical to chicken fimbrin, human
T-plastin (PLS3; 300131), and L-plastin (LCP1; 153430), respectively.
I-plastin migrated as a 68-kD protein on Western blots of human small
intestine and colon extracts. Lin et al. (1994) concluded that I-plastin
is the human homolog of chicken intestine fimbrin.
GENE FUNCTION
Lin et al. (1994) found that recombinant I-plastin crosslinked actin
filaments into bundles in the absence of calcium but not in its
presence.
MAPPING
Lin et al. (1994) mapped the I-plastin gene to chromosome 3 by PCR of
somatic cell hybrids.
*FIELD* RF
1. Lin, C.-S.; Shen, W.; Chen, Z. P.; Tu, Y.-H.; Matsudaira, P.:
Identification of I-plastin, a human fimbrin isoform expressed in
intestine and kidney. Molec. Cell. Biol. 14: 2457-2467, 1994.
*FIELD* CD
Rebekah S. Rasooly: 6/19/1998
*FIELD* ED
carol: 10/23/2009
carol: 11/3/1998
psherman: 6/19/1998
*RECORD*
*FIELD* NO
602734
*FIELD* TI
*602734 PLASTIN 1; PLS1
;;INTESTINE-SPECIFIC PLASTIN;;
I-PLASTIN;;
FIMBRIN
*FIELD* TX
read more
CLONING
Fimbrin is an actin-bundling protein that was originally discovered in
chicken intestinal brush border microvilli. By screening a human small
intestine cDNA library with a chicken fimbrin cDNA, Lin et al. (1994)
identified a cDNA encoding I-plastin. Northern blot analysis revealed
that I-plastin was expressed as a 3.7-kb mRNA in human colon and small
intestine. A survey of rat tissues detected I-plastin expression
primarily in the intestine, with a lower level in the kidneys. By
immunofluorescence, Lin et al. (1994) localized I-plastin to the brush
border of the human small intestine and colon. The predicted 629-amino
acid protein is 86%, 75%, and 73% identical to chicken fimbrin, human
T-plastin (PLS3; 300131), and L-plastin (LCP1; 153430), respectively.
I-plastin migrated as a 68-kD protein on Western blots of human small
intestine and colon extracts. Lin et al. (1994) concluded that I-plastin
is the human homolog of chicken intestine fimbrin.
GENE FUNCTION
Lin et al. (1994) found that recombinant I-plastin crosslinked actin
filaments into bundles in the absence of calcium but not in its
presence.
MAPPING
Lin et al. (1994) mapped the I-plastin gene to chromosome 3 by PCR of
somatic cell hybrids.
*FIELD* RF
1. Lin, C.-S.; Shen, W.; Chen, Z. P.; Tu, Y.-H.; Matsudaira, P.:
Identification of I-plastin, a human fimbrin isoform expressed in
intestine and kidney. Molec. Cell. Biol. 14: 2457-2467, 1994.
*FIELD* CD
Rebekah S. Rasooly: 6/19/1998
*FIELD* ED
carol: 10/23/2009
carol: 11/3/1998
psherman: 6/19/1998