LIPB2_MOUSE
ID LIPB2_MOUSE Reviewed; 882 AA.
AC O35711; Q497W6; Q7TMG4; Q8CBS6; Q99KX6;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 3.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Liprin-beta-2;
DE AltName: Full=Coiled-coil-like protein 1;
DE AltName: Full=Protein tyrosine phosphatase receptor type f polypeptide-interacting protein-binding protein 2;
DE Short=PTPRF-interacting protein-binding protein 2;
GN Name=Ppfibp2; Synonyms=Cclp1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=9199242; DOI=10.1016/s0167-4781(97)00050-x;
RA Noben-Trauth K., Naggert J.K., Nishina P.M.;
RT "Cloning and expression analysis of mouse Cclp1, a new gene encoding a
RT coiled-coil-like protein.";
RL Biochim. Biophys. Acta 1352:133-137(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Urinary bladder;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 336-882 (ISOFORM 2).
RC STRAIN=FVB/N; TISSUE=Mammary tumor, and Oocyte;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386 AND SER-502, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: May regulate the disassembly of focal adhesions. Did not bind
CC receptor-like tyrosine phosphatases type 2A (By similarity).
CC {ECO:0000250|UniProtKB:Q8ND30}.
CC -!- SUBUNIT: Forms homodimers and heterodimers.
CC {ECO:0000250|UniProtKB:Q8ND30}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=O35711-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O35711-2; Sequence=VSP_009403;
CC Name=3;
CC IsoId=O35711-3; Sequence=VSP_009401, VSP_009402;
CC Name=4;
CC IsoId=O35711-4; Sequence=VSP_009403, VSP_026136;
CC -!- TISSUE SPECIFICITY: Expressed widely. Strong expression in liver,
CC kidney, intestine, heart, lung and testis. Low expression in brain and
CC thymus. {ECO:0000269|PubMed:9199242}.
CC -!- DEVELOPMENTAL STAGE: Found at 10.5 dpc through 16.5 dpc.
CC {ECO:0000269|PubMed:9199242}.
CC -!- DOMAIN: The N-terminal coiled coil regions mediate homodimerization
CC preferentially and heterodimerization type beta/beta. The C-terminal,
CC non-coiled coil regions mediate heterodimerization type beta/alpha (By
CC similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform 3]: Due to intron retention. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the liprin family. Liprin-beta subfamily.
CC {ECO:0000305}.
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DR EMBL; U79024; AAB61902.1; -; mRNA.
DR EMBL; AK035364; BAC29047.1; -; mRNA.
DR EMBL; BC003966; AAH03966.1; -; mRNA.
DR EMBL; BC055935; AAH55935.1; -; mRNA.
DR EMBL; BC100346; AAI00347.1; -; mRNA.
DR CCDS; CCDS21691.1; -. [O35711-1]
DR CCDS; CCDS52356.1; -. [O35711-4]
DR RefSeq; NP_001157029.1; NM_001163557.1. [O35711-4]
DR RefSeq; NP_032931.2; NM_008905.2.
DR AlphaFoldDB; O35711; -.
DR SMR; O35711; -.
DR STRING; 10090.ENSMUSP00000095738; -.
DR iPTMnet; O35711; -.
DR PhosphoSitePlus; O35711; -.
DR jPOST; O35711; -.
DR MaxQB; O35711; -.
DR PaxDb; O35711; -.
DR PeptideAtlas; O35711; -.
DR PRIDE; O35711; -.
DR ProteomicsDB; 290127; -. [O35711-1]
DR ProteomicsDB; 290128; -. [O35711-2]
DR ProteomicsDB; 290129; -. [O35711-3]
DR ProteomicsDB; 290130; -. [O35711-4]
DR Antibodypedia; 1168; 141 antibodies from 24 providers.
DR DNASU; 19024; -.
DR Ensembl; ENSMUST00000098134; ENSMUSP00000095738; ENSMUSG00000036528. [O35711-4]
DR GeneID; 19024; -.
DR KEGG; mmu:19024; -.
DR UCSC; uc009jbd.2; mouse. [O35711-3]
DR UCSC; uc009jbf.1; mouse. [O35711-4]
DR UCSC; uc009jbh.2; mouse. [O35711-2]
DR CTD; 8495; -.
DR MGI; MGI:894649; Ppfibp2.
DR VEuPathDB; HostDB:ENSMUSG00000036528; -.
DR eggNOG; KOG1899; Eukaryota.
DR GeneTree; ENSGT01050000244951; -.
DR InParanoid; O35711; -.
DR OMA; WSNSGTP; -.
DR OrthoDB; 558442at2759; -.
DR PhylomeDB; O35711; -.
DR TreeFam; TF314207; -.
DR Reactome; R-MMU-388844; Receptor-type tyrosine-protein phosphatases.
DR BioGRID-ORCS; 19024; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Ppfibp2; mouse.
DR PRO; PR:O35711; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; O35711; protein.
DR Bgee; ENSMUSG00000036528; Expressed in urinary bladder urothelium and 217 other tissues.
DR ExpressionAtlas; O35711; baseline and differential.
DR GO; GO:0048786; C:presynaptic active zone; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0007528; P:neuromuscular junction development; IBA:GO_Central.
DR GO; GO:0050808; P:synapse organization; IBA:GO_Central.
DR CDD; cd09563; SAM_liprin-beta1_2_repeat1; 1.
DR CDD; cd09566; SAM_liprin-beta1_2_repeat2; 1.
DR CDD; cd09569; SAM_liprin-beta1_2_repeat3; 1.
DR Gene3D; 1.10.150.50; -; 3.
DR InterPro; IPR029515; Liprin.
DR InterPro; IPR037617; Liprin-beta_SAM_rpt_1.
DR InterPro; IPR037618; Liprin-beta_SAM_rpt_2.
DR InterPro; IPR037619; Liprin-beta_SAM_rpt_3.
DR InterPro; IPR030435; PPFIBP2.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR PANTHER; PTHR12587; PTHR12587; 1.
DR PANTHER; PTHR12587:SF18; PTHR12587:SF18; 1.
DR Pfam; PF00536; SAM_1; 2.
DR Pfam; PF07647; SAM_2; 1.
DR SMART; SM00454; SAM; 3.
DR SUPFAM; SSF47769; SSF47769; 3.
DR PROSITE; PS50105; SAM_DOMAIN; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Phosphoprotein; Reference proteome;
KW Repeat.
FT CHAIN 1..882
FT /note="Liprin-beta-2"
FT /id="PRO_0000191037"
FT DOMAIN 564..628
FT /note="SAM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT DOMAIN 636..699
FT /note="SAM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT DOMAIN 724..789
FT /note="SAM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT REGION 339..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 101..303
FT /evidence="ECO:0000250|UniProtKB:Q8ND30"
FT COMPBIAS 382..398
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..461
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..497
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 328
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8ND30"
FT MOD_RES 362
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8ND30"
FT MOD_RES 386
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 502
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 518
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8ND30"
FT VAR_SEQ 127..200
FT /note="VLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLM
FT TEVSELKLKLVGMEKEQKEQEE -> SLLPQLPQERDAQCESSVGKRWEPIYLSCAAEH
FT LPLHTSSPVGRLKLGASNEQNGPRHPGACKSAKGDEYILCH (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_009401"
FT VAR_SEQ 201..882
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_009402"
FT VAR_SEQ 459..469
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_009403"
FT VAR_SEQ 877..882
FT /note="QVGQIS -> QMAPSEGTVTQIGLLSQDIHRLTTLLSQDQLLNDPPGCP
FT (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_026136"
FT CONFLICT 4
FT /note="D -> G (in Ref. 1; AAB61902)"
FT /evidence="ECO:0000305"
FT CONFLICT 470
FT /note="R -> G (in Ref. 1; AAB61902)"
FT /evidence="ECO:0000305"
FT CONFLICT 699
FT /note="Missing (in Ref. 3; AAH03966)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 882 AA; 98753 MW; 4CD5BDF5C2F1A146 CRC64;
MTSDASHMLE AALEQMDGII AGTKTAADFS DGTCEPGLSP PSTCLNSMPV LHLIEDLRLA
LEMLALPQER EALLSQVPGP TATYIKEWFE DSLSQVNHHG AASNETYQER LARLEGDKES
LILQVSVLTD QVEAQGEKIR DLEVCLEGHQ VKLNAAEEML QQELLSRTSL ETQKLDLMTE
VSELKLKLVG MEKEQKEQEE KQRKAEELLQ ELKHLKIKVE ELENERNQYE WELKATKAEV
AQLQEQVALK DAEIERLHSQ LSRSAALHSD HAERDQEIHR LKMGMETLLV ANEDKDRRIE
ELTGLLNKYL RVKEIVMATQ GPSERTLSIN EDEIEGSFRK WNTTNKSPEE VPKQEISPRC
SSPTPGPPPL PQKSLESRAQ KKLSCSLEDL RRESGDKCVD GNQLSPVGEP KDSSFLAEQK
YPTLPGKLSG ATPNGEAAKS PPTASLQPDS SGSSQPKLNR GWSVSAPVLR DTEGGWEDIV
SSASSGTESS PQSPVTPDGK RSPKGIKKFW GKIRRTQSGN FNTDAPGMAE FRRGGLRATA
GPRLSRTRDT KGQKCDANAP FAQWSTERVC TWMEDFGLGQ YVIFARQWVT SGHTLLTATP
QDMEKELGIK HPLHRKKLVL AVKAINAKQE ETSALLDHIW VTRWLDDIGL PQYKDQFHES
RVDGRMLQYL TVNDLLFLKV TSQLHHLSIK CAIHVLHVNK FNPNCLHRRP ADESNLSPSE
VVQWSNHRVM EWLRSVDLAE YAPNLRGSGV HGGLIILEPR FTGDTLAMLL NIPPQKTLLR
RHLTTKFNAL IGPEAEQEKR DKMASPAYTP LTTTAKVRPR KLGFSHFGNM RKKKFDESTD
YICPMEPGDA VSDSHRVYGV YRGLSPLDNH ELDGLDQVGQ IS
