LOCUS       NP_061916                666 aa            linear   PRI 27-APR-2025
DEFINITION  amyloid beta A4 precursor protein-binding family B member
            1-interacting protein [Homo sapiens].
ACCESSION   NP_061916
VERSION     NP_061916.3
DBSOURCE    REFSEQ: accession NM_019043.4
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 666)
  AUTHORS   Torres-Gomez,A., Fiyouzi,T., Guerra-Espinosa,C., Cardenes,B.,
            Clares,I., Toribio,V., Reche,P.A., Cabanas,C. and Lafuente,E.M.
  TITLE     Expression of the phagocytic receptors alphaMbeta2 and alphaXbeta2
            is controlled by RIAM, VASP and Vinculin in
            neutrophil-differentiated HL-60 cells
  JOURNAL   Front Immunol 13, 951280 (2022)
   PUBMED   36238292
  REMARK    GeneRIF: Expression of the phagocytic receptors alphaMbeta2 and
            alphaXbeta2 is controlled by RIAM, VASP and Vinculin in
            neutrophil-differentiated HL-60 cells.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 666)
  AUTHORS   Sari-Ak,D., Torres-Gomez,A., Yazicioglu,Y.F., Christofides,A.,
            Patsoukis,N., Lafuente,E.M. and Boussiotis,V.A.
  TITLE     Structural, biochemical, and functional properties of the
            Rap1-Interacting Adaptor Molecule (RIAM)
  JOURNAL   Biomed J 45 (2), 289-298 (2022)
   PUBMED   34601137
  REMARK    GeneRIF: Structural, biochemical, and functional properties of the
            Rap1-Interacting Adaptor Molecule (RIAM).
            Review article
REFERENCE   3  (residues 1 to 666)
  AUTHORS   Cho,E.A., Zhang,P., Kumar,V., Kavalchuk,M., Zhang,H., Huang,Q.,
            Duncan,J.S. and Wu,J.
  TITLE     Phosphorylation of RIAM by src promotes integrin activation by
            unmasking the PH domain of RIAM
  JOURNAL   Structure 29 (4), 320-329 (2021)
   PUBMED   33275877
  REMARK    GeneRIF: Phosphorylation of RIAM by src promotes integrin
            activation by unmasking the PH domain of RIAM.
REFERENCE   4  (residues 1 to 666)
  AUTHORS   Vigouroux,C., Henriot,V. and Le Clainche,C.
  TITLE     Talin dissociates from RIAM and associates to vinculin sequentially
            in response to the actomyosin force
  JOURNAL   Nat Commun 11 (1), 3116 (2020)
   PUBMED   32561773
  REMARK    GeneRIF: Talin dissociates from RIAM and associates to vinculin
            sequentially in response to the actomyosin force.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 666)
  AUTHORS   Torres-Gomez,A., Sanchez-Trincado,J.L., Toribio,V., Torres-Ruiz,R.,
            Rodriguez-Perales,S., Yanez-Mo,M., Reche,P.A., Cabanas,C. and
            Lafuente,E.M.
  TITLE     RIAM-VASP Module Relays Integrin Complement Receptors in Outside-In
            Signaling Driving Particle Engulfment
  JOURNAL   Cells 9 (5), 1166 (2020)
   PUBMED   32397169
  REMARK    GeneRIF: RIAM-VASP Module Relays Integrin Complement Receptors in
            Outside-In Signaling Driving Particle Engulfment.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 666)
  AUTHORS   Lafuente,E.M., van Puijenbroek,A.A., Krause,M., Carman,C.V.,
            Freeman,G.J., Berezovskaya,A., Constantine,E., Springer,T.A.,
            Gertler,F.B. and Boussiotis,V.A.
  TITLE     RIAM, an Ena/VASP and Profilin ligand, interacts with Rap1-GTP and
            mediates Rap1-induced adhesion
  JOURNAL   Dev Cell 7 (4), 585-595 (2004)
   PUBMED   15469846
REFERENCE   7  (residues 1 to 666)
  AUTHORS   Deloukas,P., Earthrowl,M.E., Grafham,D.V., Rubenfield,M.,
            French,L., Steward,C.A., Sims,S.K., Jones,M.C., Searle,S.,
            Scott,C., Howe,K., Hunt,S.E., Andrews,T.D., Gilbert,J.G.,
            Swarbreck,D., Ashurst,J.L., Taylor,A., Battles,J., Bird,C.P.,
            Ainscough,R., Almeida,J.P., Ashwell,R.I., Ambrose,K.D.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Bates,K.,
            Beasley,H., Bray-Allen,S., Brown,A.J., Brown,J.Y., Burford,D.C.,
            Burrill,W., Burton,J., Cahill,P., Camire,D., Carter,N.P.,
            Chapman,J.C., Clark,S.Y., Clarke,G., Clee,C.M., Clegg,S., Corby,N.,
            Coulson,A., Dhami,P., Dutta,I., Dunn,M., Faulkner,L., Frankish,A.,
            Frankland,J.A., Garner,P., Garnett,J., Gribble,S., Griffiths,C.,
            Grocock,R., Gustafson,E., Hammond,S., Harley,J.L., Hart,E.,
            Heath,P.D., Ho,T.P., Hopkins,B., Horne,J., Howden,P.J., Huckle,E.,
            Hynds,C., Johnson,C., Johnson,D., Kana,A., Kay,M., Kimberley,A.M.,
            Kershaw,J.K., Kokkinaki,M., Laird,G.K., Lawlor,S., Lee,H.M.,
            Leongamornlert,D.A., Laird,G., Lloyd,C., Lloyd,D.M., Loveland,J.,
            Lovell,J., McLaren,S., McLay,K.E., McMurray,A.,
            Mashreghi-Mohammadi,M., Matthews,L., Milne,S., Nickerson,T.,
            Nguyen,M., Overton-Larty,E., Palmer,S.A., Pearce,A.V., Peck,A.I.,
            Pelan,S., Phillimore,B., Porter,K., Rice,C.M., Rogosin,A.,
            Ross,M.T., Sarafidou,T., Sehra,H.K., Shownkeen,R., Skuce,C.D.,
            Smith,M., Standring,L., Sycamore,N., Tester,J., Thorpe,A.,
            Torcasso,W., Tracey,A., Tromans,A., Tsolas,J., Wall,M., Walsh,J.,
            Wang,H., Weinstock,K., West,A.P., Willey,D.L., Whitehead,S.L.,
            Wilming,L., Wray,P.W., Young,L., Chen,Y., Lovering,R.C.,
            Moschonas,N.K., Siebert,R., Fechtel,K., Bentley,D., Durbin,R.,
            Hubbard,T., Doucette-Stamm,L., Beck,S., Smith,D.R. and Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 10
  JOURNAL   Nature 429 (6990), 375-381 (2004)
   PUBMED   15164054
REFERENCE   8  (residues 1 to 666)
  AUTHORS   Inagaki,T., Suzuki,S., Miyamoto,T., Takeda,T., Yamashita,K.,
            Komatsu,A., Yamauchi,K. and Hashizume,K.
  TITLE     The retinoic acid-responsive proline-rich protein is identified in
            promyeloleukemic HL-60 cells
  JOURNAL   J Biol Chem 278 (51), 51685-51692 (2003)
   PUBMED   14530287
  REMARK    GeneRIF: all-trans-retinoic acid-inducible RARP1 selectively
            affects signal transduction and may contribute to myeloid and
            megakaryocytic differentiation.(RARP1)
REFERENCE   9  (residues 1 to 666)
  AUTHORS   Ermekova,K.S., Zambrano,N., Linn,H., Minopoli,G., Gertler,F.,
            Russo,T. and Sudol,M.
  TITLE     The WW domain of neural protein FE65 interacts with proline-rich
            motifs in Mena, the mammalian homolog of Drosophila enabled
  JOURNAL   J Biol Chem 272 (52), 32869-32877 (1997)
   PUBMED   9407065
REFERENCE   10 (residues 1 to 666)
  AUTHORS   Law,D.A., Nannizzi-Alaimo,L. and Phillips,D.R.
  TITLE     Outside-in integrin signal transduction. Alpha IIb beta 3-(GP IIb
            IIIa) tyrosine phosphorylation induced by platelet aggregation
  JOURNAL   J Biol Chem 271 (18), 10811-10815 (1996)
   PUBMED   8631894
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BM150270.1, BM556115.1 and BC054516.1.
            
            On Nov 29, 2004 this sequence version replaced NP_061916.2.
            
            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##
            CDS exon combination :: BC054516.1, AY152730.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA1965299, SAMEA1966682 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000376236.9/ ENSP00000365411.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..666
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10p12.1"
     Protein         1..666
                     /product="amyloid beta A4 precursor protein-binding family
                     B member 1-interacting protein"
                     /note="proline rich EVH1 ligand 1; Rap1-GTP-interacting
                     adaptor molecule; retinoic acid-responsive proline-rich
                     protein 1; proline-rich protein 73; Rap1-interacting
                     adaptor molecule; PREL-1; RARP-1; APBB1-interacting
                     protein 1; rap1-GTP-interacting adapter molecule;
                     MLLT10/APBB1IP reciprocal fusion; MLLT10/APBB1IP
                     reciprocal fusion protein"
                     /calculated_mol_wt=73052
     Site            55
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q7Z5R6.1)"
     Region          122..155
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z5R6.1)"
     Region          183..264
                     /region_name="RA_MRL_RIAM"
                     /note="Ras-associating (RA) domain found in
                     Rap1-GTP-interacting adapter molecule (RIAM); cd16137"
                     /db_xref="CDD:340554"
     Site            order(186..193,209..212,227,245..246,249)
                     /site_type="other"
                     /note="RA-PH-RAP1 interaction site [polypeptide binding]"
                     /db_xref="CDD:340554"
     Region          307..428
                     /region_name="PH_APBB1IP"
                     /note="Amyloid beta (A4) Precursor protein-Binding, family
                     B, member 1 Interacting Protein pleckstrin homology (PH)
                     domain; cd01259"
                     /db_xref="CDD:269961"
     Region          448..666
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z5R6.1)"
     Site            526
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z5R6.1)"
     Site            528
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8R5A3; propagated from
                     UniProtKB/Swiss-Prot (Q7Z5R6.1)"
     Site            531
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8R5A3; propagated from
                     UniProtKB/Swiss-Prot (Q7Z5R6.1)"
     CDS             1..666
                     /gene="APBB1IP"
                     /gene_synonym="INAG1; PREL1; RARP1; RIAM"
                     /coded_by="NM_019043.4:318..2318"
                     /db_xref="CCDS:CCDS31167.1"
                     /db_xref="GeneID:54518"
                     /db_xref="HGNC:HGNC:17379"
                     /db_xref="MIM:609036"
ORIGIN      
        1 mgessedidq mfstllgemd lltqslgvdt lpppdpnppr aefnysvgfk dlneslnale
       61 dqdldalmad lvadiseaeq rtiqaqkesl qnqhhsaslq asifsgaasl gygtnvaatg
      121 isqyeddlpp ppadpvldlp lpppppepls qeeeeaqaka dkiklalekl keakvkklvv
      181 kvhmndnstk slmvderqla rdvldnlfek thcdcnvdwc lyeiypelqi erffedhenv
      241 vevlsdwtrd tenkilflek eekyavfknp qnfyldnrgk kesketnekm naknkeslle
      301 esfcgtsiiv pelegalylk edgkkswkrr yfllrasgiy yvpkgktkts rdlacfiqfe
      361 nvniyygtqh kmkykaptdy cfvlkhpqiq kesqyikylc cddtrtlnqw vmgiriakyg
      421 ktlydnyqra vakaglasrw tnlgtvnaaa paqpstgpkt gttqpngqip qathsvsavl
      481 qeaqrhaets kdkkpalgnh hdpavpraph apksslpppp pvrrssdtsg spatplkakg
      541 tgggglpapp ddflpppppp pplddpelpp pppdfmeppp dfvpppppsy agiagselpp
      601 ppppppapap apvpdsarpp pavakrppvp pkrqenpghp ggagggeqdf msdlmkalqk
      661 krgnvs
//
