LIPA3_RAT
ID LIPA3_RAT Reviewed; 1192 AA.
AC Q91Z79;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-FEB-2004, sequence version 2.
DT 25-MAY-2022, entry version 130.
DE RecName: Full=Liprin-alpha-3;
DE AltName: Full=Protein tyrosine phosphatase receptor type f polypeptide-interacting protein alpha-3;
DE Short=PTPRF-interacting protein alpha-3;
GN Name=Ppfia3;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 1-992, AND INTERACTION WITH RIMS1 AND RIMS2.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=11797009; DOI=10.1038/415321a;
RA Schoch S., Castillo P.E., Jo T., Mukherjee K., Geppert M., Wang Y.,
RA Schmitz F., Malenka R.C., Suedhof T.C.;
RT "RIM1alpha forms a protein scaffold for regulating neurotransmitter release
RT at the active zone.";
RL Nature 415:321-326(2002).
RN [3]
RP PROTEIN SEQUENCE OF 172-180; 305-310 AND 361-367, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
RN [4]
RP INTERACTION WITH RIMS3 AND RIMS4.
RX PubMed=12620390; DOI=10.1016/s0888-7543(02)00024-1;
RA Wang Y., Suedhof T.C.;
RT "Genomic definition of RIM proteins: evolutionary amplification of a family
RT of synaptic regulatory proteins.";
RL Genomics 81:126-137(2003).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY, AND MASS
RP SPECTROMETRY.
RC STRAIN=Holtzman; TISSUE=Sperm;
RX PubMed=20966424; DOI=10.2164/jandrol.110.010967;
RA Suryawanshi A.R., Khan S.A., Gajbhiye R.K., Gurav M.Y., Khole V.V.;
RT "Differential proteomics leads to identification of domain specific
RT epididymal sperm proteins.";
RL J. Androl. 32:240-259(2011).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142; THR-712; THR-790 AND
RP SER-792, 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 [7]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP INDUCTION.
RX PubMed=23124857; DOI=10.1007/s00418-012-1044-y;
RA Joshi C.S., Suryawanshi A.R., Khan S.A., Balasinor N.H., Khole V.V.;
RT "Liprin alpha3: a putative estrogen regulated acrosomal protein.";
RL Histochem. Cell Biol. 139:535-548(2013).
CC -!- FUNCTION: May regulate the disassembly of focal adhesions. May localize
CC receptor-like tyrosine phosphatases type 2A at specific sites on the
CC plasma membrane, possibly regulating their interaction with the
CC extracellular environment and their association with substrates.
CC {ECO:0000250|UniProtKB:O75145}.
CC -!- SUBUNIT: Forms homodimers and heterodimers with liprins-alpha and
CC liprins-beta. Interacts with the second PTPase domain of PTPRD, PTPRF
CC and PTPRS. Binds RIMS1, RIMS2, RIMS3 and RIMS4.
CC {ECO:0000269|PubMed:11797009, ECO:0000269|PubMed:12620390}.
CC -!- INTERACTION:
CC Q91Z79; P97879: Grip1; NbExp=3; IntAct=EBI-8276993, EBI-936113;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23124857}.
CC Cytoplasmic vesicle, secretory vesicle, acrosome
CC {ECO:0000269|PubMed:23124857}. Note=Also detected in epididymosome.
CC {ECO:0000269|PubMed:23124857}.
CC -!- TISSUE SPECIFICITY: Expressed in the head of epididymal sperm but not
CC in testicular sperm (at protein level) (PubMed:20966424,
CC PubMed:23124857). Also detected in epididymis, brain, intestine and
CC lungs (PubMed:23124857). {ECO:0000269|PubMed:20966424,
CC ECO:0000269|PubMed:23124857}.
CC -!- DEVELOPMENTAL STAGE: First detected at postnatal day 20 and 40 in
CC testis and epididymis respectively. {ECO:0000269|PubMed:23124857}.
CC -!- INDUCTION: Down-regulated by tamoxifen. {ECO:0000269|PubMed:23124857}.
CC -!- DOMAIN: The N-terminal coiled coil regions mediate homodimerization
CC preferentially and heterodimerization type alpha/alpha. The C-terminal,
CC non-coiled coil regions mediate heterodimerization type alpha/beta and
CC interaction with PTPRD, PTPRF and PTPRS.
CC {ECO:0000250|UniProtKB:O75145}.
CC -!- MASS SPECTROMETRY: Mass=133436.8; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:20966424};
CC -!- SIMILARITY: Belongs to the liprin family. Liprin-alpha subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL23696.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AABR03000917; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AY057065; AAL23696.1; ALT_INIT; mRNA.
DR AlphaFoldDB; Q91Z79; -.
DR SMR; Q91Z79; -.
DR CORUM; Q91Z79; -.
DR IntAct; Q91Z79; 1.
DR MINT; Q91Z79; -.
DR STRING; 10116.ENSRNOP00000028142; -.
DR iPTMnet; Q91Z79; -.
DR PhosphoSitePlus; Q91Z79; -.
DR SwissPalm; Q91Z79; -.
DR jPOST; Q91Z79; -.
DR PaxDb; Q91Z79; -.
DR PRIDE; Q91Z79; -.
DR UCSC; RGD:620054; rat.
DR RGD; 620054; Ppfia3.
DR eggNOG; KOG0249; Eukaryota.
DR InParanoid; Q91Z79; -.
DR PhylomeDB; Q91Z79; -.
DR Reactome; R-RNO-181429; Serotonin Neurotransmitter Release Cycle.
DR Reactome; R-RNO-181430; Norepinephrine Neurotransmitter Release Cycle.
DR Reactome; R-RNO-210500; Glutamate Neurotransmitter Release Cycle.
DR Reactome; R-RNO-212676; Dopamine Neurotransmitter Release Cycle.
DR Reactome; R-RNO-264642; Acetylcholine Neurotransmitter Release Cycle.
DR Reactome; R-RNO-388844; Receptor-type tyrosine-protein phosphatases.
DR PRO; PR:Q91Z79; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0001669; C:acrosomal vesicle; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0098875; C:epididymosome; IDA:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0048786; C:presynaptic active zone; IBA:GO_Central.
DR GO; GO:0098831; C:presynaptic active zone cytoplasmic component; ISO:RGD.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0007269; P:neurotransmitter secretion; IMP:RGD.
DR GO; GO:0048172; P:regulation of short-term neuronal synaptic plasticity; IMP:RGD.
DR GO; GO:0050808; P:synapse organization; IBA:GO_Central.
DR GO; GO:0016081; P:synaptic vesicle docking; ISO:RGD.
DR GO; GO:0016079; P:synaptic vesicle exocytosis; ISO:RGD.
DR CDD; cd09562; SAM_liprin-alpha1_2_3_4_repeat1; 1.
DR CDD; cd09565; SAM_liprin-alpha1_2_3_4_repeat2; 1.
DR CDD; cd09568; SAM_liprin-alpha1_2_3_4_repeat3; 1.
DR Gene3D; 1.10.150.50; -; 3.
DR InterPro; IPR029515; Liprin.
DR InterPro; IPR037620; Liprin-alpha_SAM_rpt_1.
DR InterPro; IPR037621; Liprin-alpha_SAM_rpt_2.
DR InterPro; IPR037622; Liprin-alpha_SAM_rpt_3.
DR InterPro; IPR030440; PPFIA3.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR PANTHER; PTHR12587; PTHR12587; 1.
DR PANTHER; PTHR12587:SF4; PTHR12587:SF4; 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 Coiled coil; Cytoplasm; Cytoplasmic vesicle; Direct protein sequencing;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..1192
FT /note="Liprin-alpha-3"
FT /id="PRO_0000191031"
FT DOMAIN 836..902
FT /note="SAM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT DOMAIN 951..1015
FT /note="SAM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT DOMAIN 1039..1108
FT /note="SAM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 521..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 623..815
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1155..1192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 26..133
FT /evidence="ECO:0000255"
FT COILED 161..501
FT /evidence="ECO:0000255"
FT COILED 595..643
FT /evidence="ECO:0000255"
FT COILED 1012..1038
FT /evidence="ECO:0000255"
FT COMPBIAS 543..557
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 637..672
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1172..1192
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75145"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 207
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75145"
FT MOD_RES 431
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13136"
FT MOD_RES 507
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P60469"
FT MOD_RES 639
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13136"
FT MOD_RES 644
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P60469"
FT MOD_RES 667
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13136"
FT MOD_RES 682
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75145"
FT MOD_RES 712
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 735
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13136"
FT MOD_RES 790
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 792
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1121
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13136"
FT MOD_RES 1162
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75145"
SQ SEQUENCE 1192 AA; 133429 MW; 990C7582667D23EA CRC64;
MMCEVMPTIS EDGRRGSALG PDDAGGELER LMVTMLTERE RLLETLREAQ DGLATAQLRL
RELGHEKDSL QRQLSIALPQ EFAALTKELN LCREQLLERE EEIAELKAER NNTRLLLEHL
ECLVSRHERS LRMTVVKRQA QSPGGVSSEV EVLKALKSLF EHHKALDEKV RERLRMALER
VAVLEEELEL SNQEALNLRD QLSRRRSGLE EPGKDGDGQT LANGLGPVGE SSRRTAELEE
ALERQRAEVC QLRERLAVLC RQMSQLEEEL GTAHRELGKA EEANSKLQRD LKEALAQRED
MEERITTLEK RYLSAQREAT SLHDANDKLE NELASKESLY RQSEEKSRQL AEWLDDAKQK
LQQTLQKAET LPEIEAQLAQ RVAALNKAEE RHGNFEERLR QLEAQLEEKN QELQRARQRE
KMNDDHNKRL SETVDKLLSE SNERLQLHLK ERMGALEEKN SLSEEIANMK KLQDELLLNK
EQLLAEMERM QMEIDQLRGR PPSYSRSLPG SALELRYSQA PTLPSGAPLD PYGAGSGRAG
KRGRWSGAKD ESSKDWDRST PAGSIPPPFP GELDGSDEEE TEGMFGAELL SPSGQADVQT
LAIMLQEQLE AINKEIKLIQ EEKETTEQRA EELESRVSSS GLDSLGRYRS SCSLPPSLTT
STLASPSPPS SGHSTPRLAP PSPARETDKT NHVPKDEAGV PRGEGPAIPG DTPPPTPRSA
RLERMTQALA LQAGSLEDGA PPRGSESTPD SLHKAPKRKS IKSSIGRLFG KKEKGRMGPP
GRESVSLAGT PSDETLATDP LGLAKLTGPG DKDRRNKRKH ELLEEACRQG LPFAAWDGPT
VVSWLELWVG MPAWYVAACR ANVKSGAIMA NLSDTEIQRE IGISNPLHRL KLRLAIQEMV
SLTSPSAPAS SRTPTGNVWM THEEMESLTA ATKPETKEIS WEQILAYGDM NHEWVGNDWL
PSLGLPQYRS YFMESLVDAR MLDHLNKKEL REQLKMVDSF HRVSLHYGIM CLKRLNYDRK
DLERRREESQ TQIRDVMVWS NERVMGWVSG LGLKEFATNL TESGVHGALL ALDETFDYSD
LALLLQIPTQ NAQARQLLEK EFSNLISLGT DRRLDEDSAK SFSRSPSWRK MFREKDLRGV
TPDSAEMLPP NFRSAAAGAL GSPGLPLRKL QPEGQTSGSS RADGVSVRTY SC
