LOCUS       NP_003617               1202 aa            linear   PRI 30-APR-2025
DEFINITION  liprin-alpha-1 isoform b [Homo sapiens].
ACCESSION   NP_003617
VERSION     NP_003617.1
DBSOURCE    REFSEQ: accession NM_003626.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1202)
  AUTHORS   Pehkonen,H., Filippou,A., Vaananen,J., Lindfors,I., Vanttinen,M.,
            Ianevski,P., Makela,A., Munne,P., Klefstrom,J., Toppila-Salmi,S.,
            Grenman,R., Hagstrom,J., Makitie,A.A., Karhemo,P.R. and Monni,O.
  TITLE     Liprin-alpha1 contributes to oncogenic MAPK signaling by
            counteracting ERK activity
  JOURNAL   Mol Oncol 18 (3), 662-676 (2024)
   PUBMED   38264964
  REMARK    GeneRIF: Liprin-alpha1 contributes to oncogenic MAPK signaling by
            counteracting ERK activity.
REFERENCE   2  (residues 1 to 1202)
  AUTHORS   Gao,Y., Guan,L., Jia,R., Xiao,W., Han,Y., Li,Y., Tang,P., Yu,Z. and
            Zhang,H.
  TITLE     High expression of PPFIA1 in human esophageal squamous cell
            carcinoma correlates with tumor metastasis and poor prognosis
  JOURNAL   BMC Cancer 23 (1), 417 (2023)
   PUBMED   37158817
  REMARK    GeneRIF: High expression of PPFIA1 in human esophageal squamous
            cell carcinoma correlates with tumor metastasis and poor prognosis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1202)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 1202)
  AUTHORS   Liang,M., Jin,G., Xie,X., Zhang,W., Li,K., Niu,F., Yu,C. and Wei,Z.
  TITLE     Oligomerized liprin-alpha promotes phase separation of ELKS for
            compartmentalization of presynaptic active zone proteins
  JOURNAL   Cell Rep 34 (12), 108901 (2021)
   PUBMED   33761347
  REMARK    GeneRIF: Oligomerized liprin-alpha promotes phase separation of
            ELKS for compartmentalization of presynaptic active zone proteins.
            Erratum:[Cell Rep. 2021 Jul 27;36(4):109476. doi:
            10.1016/j.celrep.2021.109476. PMID: 34320361]
REFERENCE   5  (residues 1 to 1202)
  AUTHORS   Clapero,F., Tortarolo,D., Valdembri,D. and Serini,G.
  TITLE     Quantifying Polarized Extracellular Matrix Secretion in Cultured
            Endothelial Cells
  JOURNAL   Methods Mol Biol 2217, 301-311 (2021)
   PUBMED   33215388
  REMARK    GeneRIF: Quantifying Polarized Extracellular Matrix Secretion in
            Cultured Endothelial Cells.
REFERENCE   6  (residues 1 to 1202)
  AUTHORS   Ko,J., Kim,S., Valtschanoff,J.G., Shin,H., Lee,J.R., Sheng,M.,
            Premont,R.T., Weinberg,R.J. and Kim,E.
  TITLE     Interaction between liprin-alpha and GIT1 is required for AMPA
            receptor targeting
  JOURNAL   J Neurosci 23 (5), 1667-1677 (2003)
   PUBMED   12629171
REFERENCE   7  (residues 1 to 1202)
  AUTHORS   Wyszynski,M., Kim,E., Dunah,A.W., Passafaro,M., Valtschanoff,J.G.,
            Serra-Pages,C., Streuli,M., Weinberg,R.J. and Sheng,M.
  TITLE     Interaction between GRIP and liprin-alpha/SYD2 is required for AMPA
            receptor targeting
  JOURNAL   Neuron 34 (1), 39-52 (2002)
   PUBMED   11931740
REFERENCE   8  (residues 1 to 1202)
  AUTHORS   Serra-Pages,C., Medley,Q.G., Tang,M., Hart,A. and Streuli,M.
  TITLE     Liprins, a family of LAR transmembrane protein-tyrosine
            phosphatase-interacting proteins
  JOURNAL   J Biol Chem 273 (25), 15611-15620 (1998)
   PUBMED   9624153
REFERENCE   9  (residues 1 to 1202)
  AUTHORS   Pulido,R., Serra-Pages,C., Tang,M. and Streuli,M.
  TITLE     The LAR/PTP delta/PTP sigma subfamily of transmembrane
            protein-tyrosine-phosphatases: multiple human LAR, PTP delta, and
            PTP sigma isoforms are expressed in a tissue-specific manner and
            associate with the LAR-interacting protein LIP.1
  JOURNAL   Proc Natl Acad Sci U S A 92 (25), 11686-11690 (1995)
   PUBMED   8524829
REFERENCE   10 (residues 1 to 1202)
  AUTHORS   Serra-Pages,C., Kedersha,N.L., Fazikas,L., Medley,Q., Debant,A. and
            Streuli,M.
  TITLE     The LAR transmembrane protein tyrosine phosphatase and a
            coiled-coil LAR-interacting protein co-localize at focal adhesions
  JOURNAL   EMBO J 14 (12), 2827-2838 (1995)
   PUBMED   7796809
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AP002336.5, AP000487.6 and KC877433.1.
            
            Summary: The protein encoded by this gene is a member of the LAR
            protein-tyrosine phosphatase-interacting protein (liprin) family.
            Liprins interact with members of LAR family of transmembrane
            protein tyrosine phosphatases, which are known to be important for
            axon guidance and mammary gland development. This protein binds to
            the intracellular membrane-distal phosphatase domain of tyrosine
            phosphatase LAR, and appears to localize LAR to cell focal
            adhesions. This interaction may regulate the disassembly of focal
            adhesion and thus help orchestrate cell-matrix interactions.
            Alternatively spliced transcript variants encoding distinct
            isoforms have been described. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) represents the longest
            transcript and it encodes the longer protein (isoform b).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC034046.1, U22816.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000253925.12/ ENSP00000253925.7
            RefSeq Select criteria :: based on manual assertion, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1202
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.3"
     Protein         1..1202
                     /product="liprin-alpha-1 isoform b"
                     /note="Liprin-alpha1; LAR-interacting protein 1;
                     liprin-alpha-1; LIP-1; protein tyrosine phosphatase
                     receptor type f polypeptide-interacting protein alpha-1;
                     protein tyrosine phosphatase, receptor type, f polypeptide
                     (PTPRF), interacting protein (liprin), alpha 1"
                     /calculated_mol_wt=135648
     Region          1..33
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13136.1)"
     Region          <45..662
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Site            150
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13136.1)"
     Region          224..245
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13136.1)"
     Site            230
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q13136.1)"
     Site            239
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q13136.1)"
     Site            242
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13136.1)"
     Region          <243..>523
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Site            244
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q13136.1)"
     Region          426..446
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13136.1)"
     Site            448
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q13136.1)"
     Region          651..855
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13136.1)"
     Site            666
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13136.1)"
     Site            668
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q13136.1)"
     Site            693
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13136.1)"
     Site            761
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q13136.1)"
     Site            763
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13136.1)"
     Region          875..945
                     /region_name="SAM_liprin-alpha1,2,3,4_repeat1"
                     /note="SAM domain of liprin-alpha1,2,3,4 proteins repeat
                     1; cd09562"
                     /db_xref="CDD:188961"
     Region          962..1027
                     /region_name="SAM_liprin-alpha1,2,3,4_repeat2"
                     /note="SAM domain of liprin-alpha1,2,3,4 proteins repeat
                     2; cd09565"
                     /db_xref="CDD:188964"
     Region          1047..1118
                     /region_name="SAM_liprin-alpha1,2,3,4_repeat3"
                     /note="SAM domain of liprin-alpha1,2,3,4 proteins repeat
                     3; cd09568"
                     /db_xref="CDD:188967"
     Site            1133
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13136.1)"
     Site            1159
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q13136.1)"
     Region          1163..1202
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13136.1)"
     CDS             1..1202
                     /gene="PPFIA1"
                     /gene_synonym="LIP.1; LIP1; LIPRIN"
                     /coded_by="NM_003626.5:226..3834"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS31627.1"
                     /db_xref="GeneID:8500"
                     /db_xref="HGNC:HGNC:9245"
                     /db_xref="MIM:611054"
ORIGIN      
        1 mmcevmptis eaegppgggg ghgsgspsqp dadshfeqlm vsmleerdrl ldtlretqet
       61 laltqgklhe vgherdslqr qlntalpqef aaltkelnvc reqllereee iaelkaernn
      121 trlllehlec lvsrherslr mtvvkrqaqs pagvssevev lkalkslfeh hkaldekvre
      181 rlrvalercs lleeelgath kelmilkeqn nqkktltdgv ldinheqent pstsgkrssd
      241 gslsheedla kvielqeiis kqsreqsqmk erlaslsshv teleedldta rkdlikseem
      301 ntklqrdvre amaqkedmee rittlekryl aaqreatsvh dlndklenei ankdsmhrqt
      361 edknrqlqer lelaeqklqq tlrkaetlpe veaelaqrva alskaeerhg nieerlrqme
      421 aqleeknqel qrarqrekmn eehnkrlsdt vdkllsesne rlqlhlkerm aaledknsll
      481 revesakkql eetqhdkdql vlniealrae ldhmrlrgas lhhgrphlgs vpdfrfpmad
      541 ghtdsystsa vlrrpqkgrl aalrdepskv qtlneqdwer aqqasvlanv aqafesdadv
      601 sdgeddrdtl lssvdllsps gqadahtlam mlqeqldain keirliqeek enteqraeei
      661 esrvgsgsld nlgrfrsmss ippypassla sssppgsgrs tprriphspa revdrlgvmt
      721 llppsreevr ddkttikcet sppsspralr ldrlhkgalh tvshedirdi rnstgsqdgp
      781 vsnpsssnss qdslhkapkk kgikssigrl fgkkekgrpg qtgkealgqa gvsetdnssq
      841 dalglsklgg qaeknrklqk khelleearr qglpfaqwdg ptvvvwlelw vgmpawyvaa
      901 cranvksgai msalsdteiq reigisnplh rlklrlaiqe imsltspsap ptsrttlayg
      961 dmnhewigne wlpslglpqy rsyfmeclvd armldhltkk dlrgqlkmvd sfhrnsfqcg
     1021 imclrrlnyd rkelerkree sqseikdvlv wsndrvirwi lsiglkeyan nliesgvhga
     1081 llaldetfdf salalllqip tqntqaravl erefnnllvm gtdrrfdedd dksfrrapsw
     1141 rkkfrpkdir glaagsaetl panfrvtssm sspsmqpkkm qmdgnvsgtq rldsatvrty
     1201 sc
//
