LOCUS       NP_055880               1989 aa            linear   PRI 04-JUN-2025
DEFINITION  exophilin-5 isoform 1 [Homo sapiens].
ACCESSION   NP_055880
VERSION     NP_055880.2
DBSOURCE    REFSEQ: accession NM_015065.3
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 1989)
  AUTHORS   Yang,Y., Cao,Y., Han,X., Ma,X., Li,R., Wang,R., Xiao,L. and Xie,L.
  TITLE     Revealing EXPH5 as a potential diagnostic gene biomarker of the
            late stage of COPD based on machine learning analysis
  JOURNAL   Comput Biol Med 154, 106621 (2023)
   PUBMED   36746116
  REMARK    GeneRIF: Revealing EXPH5 as a potential diagnostic gene biomarker
            of the late stage of COPD based on machine learning analysis.
REFERENCE   2  (residues 1 to 1989)
  AUTHORS   Kim,H.J., Kim,E., Lee,H., Jung,J.W., Kim,J.E., Pack,C.G. and
            Lee,J.W.
  TITLE     SLAC2B-dependent microtubule acetylation regulates extracellular
            matrix-mediated intracellular TM4SF5 traffic to the plasma
            membranes
  JOURNAL   FASEB J 35 (3), e21369 (2021)
   PUBMED   33554392
  REMARK    GeneRIF: SLAC2B-dependent microtubule acetylation regulates
            extracellular matrix-mediated intracellular TM4SF5 traffic to the
            plasma membranes.
REFERENCE   3  (residues 1 to 1989)
  AUTHORS   Bare,Y., Chan,G.K., Hayday,T., McGrath,J.A. and Parsons,M.
  TITLE     Slac2-b Coordinates Extracellular Vesicle Secretion to Regulate
            Keratinocyte Adhesion and Migration
  JOURNAL   J Invest Dermatol 141 (3), 523-532 (2021)
   PUBMED   32890627
  REMARK    GeneRIF: Slac2-b Coordinates Extracellular Vesicle Secretion to
            Regulate Keratinocyte Adhesion and Migration.
REFERENCE   4  (residues 1 to 1989)
  AUTHORS   McGrath,J.A., Stone,K.L., Begum,R., Simpson,M.A.,
            Dopping-Hepenstal,P.J., Liu,L., McMillan,J.R., South,A.P.,
            Pourreyron,C., McLean,W.H., Martinez,A.E., Mellerio,J.E. and
            Parsons,M.
  TITLE     Germline Mutation in EXPH5 Implicates the Rab27B Effector Protein
            Slac2-b in Inherited Skin Fragility
  JOURNAL   Am J Hum Genet 91 (6), 1115-1121 (2012)
   PUBMED   23176819
  REMARK    GeneRIF: our findings identify an unexpected role for Slac2-b in
            inherited skin fragility and expand the clinical spectrum of human
            disorders of GTPase effector proteins.
REFERENCE   5  (residues 1 to 1989)
  AUTHORS   Ostrowski,M., Carmo,N.B., Krumeich,S., Fanget,I., Raposo,G.,
            Savina,A., Moita,C.F., Schauer,K., Hume,A.N., Freitas,R.P.,
            Goud,B., Benaroch,P., Hacohen,N., Fukuda,M., Desnos,C.,
            Seabra,M.C., Darchen,F., Amigorena,S., Moita,L.F. and Thery,C.
  TITLE     Rab27a and Rab27b control different steps of the exosome secretion
            pathway
  JOURNAL   Nat Cell Biol 12 (1), 19-30 (2010)
   PUBMED   19966785
REFERENCE   6  (residues 1 to 1989)
  AUTHORS   Kondo,H., Shirakawa,R., Higashi,T., Kawato,M., Fukuda,M., Kita,T.
            and Horiuchi,H.
  TITLE     Constitutive GDP/GTP exchange and secretion-dependent GTP
            hydrolysis activity for Rab27 in platelets
  JOURNAL   J Biol Chem 281 (39), 28657-28665 (2006)
   PUBMED   16880209
REFERENCE   7  (residues 1 to 1989)
  AUTHORS   Fukuda,M.
  TITLE     Slp4-a/granuphilin-a inhibits dense-core vesicle exocytosis through
            interaction with the GDP-bound form of Rab27A in PC12 cells
  JOURNAL   J Biol Chem 278 (17), 15390-15396 (2003)
   PUBMED   12590134
REFERENCE   8  (residues 1 to 1989)
  AUTHORS   Nagashima,K., Torii,S., Yi,Z., Igarashi,M., Okamoto,K., Takeuchi,T.
            and Izumi,T.
  TITLE     Melanophilin directly links Rab27a and myosin Va through its
            distinct coiled-coil regions
  JOURNAL   FEBS Lett 517 (1-3), 233-238 (2002)
   PUBMED   12062444
REFERENCE   9  (residues 1 to 1989)
  AUTHORS   Kuroda,T.S., Fukuda,M., Ariga,H. and Mikoshiba,K.
  TITLE     The Slp homology domain of synaptotagmin-like proteins 1-4 and
            Slac2 functions as a novel Rab27A binding domain
  JOURNAL   J Biol Chem 277 (11), 9212-9218 (2002)
   PUBMED   11773082
  REMARK    GeneRIF: Slac2-b/KIAA0624 contains an N-terminal Slp homology
            domain (SHD) (PMID: 11327731). The SHD of Slac2-b specifically and
            directly binds the GTP-bound form of Rab27A (J. Biol. Chem. 277,
            (2002) 9212-9218; PMID: 11773082).
REFERENCE   10 (residues 1 to 1989)
  AUTHORS   So,J.Y. and Teng,J.
  TITLE     Epidermolysis Bullosa Simplex
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301543
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP002453.4, BP358360.1,
            BC117701.1, KF455497.1, AP005718.3 and AI203086.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jan 24, 2009 this sequence version replaced NP_055880.1.
            
            Summary: The protein encoded by this gene is a member of the
            synaptotagmin-like protein (Slp) family lacking a C2 domain. It
            contains an N-terminal synaptotagmin-like homology domain (SHD),
            and is a ras-related protein Rab-27B effector protein. This protein
            is thought to be involved in exosome secretion and intracellular
            vesicle trafficking. Reduced expression of this gene results in
            keratin filament defects. Mutations in this gene have been
            associated with some cases of epidermolysis bullosa, an inherited
            skin fragility disorder. Alternative splicing results in multiple
            transcript variants encoding different isoforms. [provided by
            RefSeq, Aug 2015].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            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 :: AY099469.1, BC113119.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000265843.9/ ENSP00000265843.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1989
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q22.3"
     Protein         1..1989
                     /product="exophilin-5 isoform 1"
                     /note="synaptotagmin-like homologue lacking C2 domains b;
                     slp homolog lacking C2 domains b; synaptotagmin-like
                     protein homolog lacking C2 domains b"
                     /calculated_mol_wt=222390
     Region          93..117
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NEV8.4)"
     Region          348..391
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NEV8.4)"
     Site            603
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NEV8.4)"
     Region          631..651
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NEV8.4)"
     Region          806..827
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NEV8.4)"
     Site            806
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NEV8.4)"
     Site            809
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NEV8.4)"
     Region          882..933
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NEV8.4)"
     Site            1028
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NEV8.4)"
     Site            1086
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NEV8.4)"
     Region          1094..1113
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NEV8.4)"
     Region          1124..1152
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NEV8.4)"
     Site            1124
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NEV8.4)"
     Region          1365..1493
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NEV8.4)"
     Site            1505
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NEV8.4)"
     Region          1521..1590
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NEV8.4)"
     Region          1644..1737
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NEV8.4)"
     Site            1753
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8NEV8.4)"
     Site            1768
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NEV8.4)"
     Site            1821
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NEV8.4)"
     Site            1851
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NEV8.4)"
     Region          1921..1989
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NEV8.4)"
     CDS             1..1989
                     /gene="EXPH5"
                     /gene_synonym="EBS4; SLAC2-B; SLAC2B"
                     /coded_by="NM_015065.3:233..6202"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS8341.1"
                     /db_xref="GeneID:23086"
                     /db_xref="HGNC:HGNC:30578"
                     /db_xref="MIM:612878"
ORIGIN      
        1 mtkvppafdf sflndeeark ilqvlernee lqraekdris klqktkrdir wlqgvtgewf
       61 eeiqrkkfcn etdvsqmlkq pltyrlskem akndpielpt srsknvtnqk kptpfssrms
      121 frssfaslfs frksgketsk lpslgqkgcd ghagppmpvr gaavqakiyn splenhlvds
      181 tfvpkpavmr eesgmpppwd aslleneffq vlddldskla qeqsassvnt rtplnygsrt
      241 qfghfyssgn rhgniterhk khynetsnms iydilrpgtp regfktfspr tstiydmyrt
      301 reprvfkedy vqkntfgsts lcfdsrqrsa lpatghftar slhfpattqs ksgfipprhq
      361 qspkrtplss iiwnrsdssr drenqeeflr apspmeidpa dkyvyprgfq enkryesyhs
      421 qnvyqrvsln apmenamspd tfensenmpf yhqsntftrs ffsntfgrsg eqrrfgqgpf
      481 wgqekghsfw sdfhrsrksf sssdrdfemi smeansvsai hghnvssehw esfssgygtd
      541 vsrgqeephp wqfdfqrstl dsmvvshgne tqltphfgtp nvcsmtgssy hvksselvsq
      601 qdsspvevhi nkeassfgia qtlassfkts fsqisddrrn pqspnlqnpt vtlqkifpnk
      661 pashpmrsht evtvtssnsv dslplaksqp nilvtevnne kdlnesisee dkqlskmdqt
      721 nkageipqpv sqtgisnslp dfqnplsqds aksngfgfna stiisskksp rvfsrkdtsk
      781 myiphtdksn dikqdkrfte nrklgstasl pfiqehrtpp sfprtdqgch qeltvnnedi
      841 sriitnnhws saltdtqnaq yskckltpgh ktscdsldls saalpdssps knssldapvv
      901 psttvfsrrs psdkdpslge reekdnagkn qknqfivshs enqerndspv pthdevvdvk
      961 chshspfrne rgkgkirhhi scieklskte sisvptsdhr slieanqsns kvseldtiyc
     1021 tlprksssfl ihgrqsgski maaslrngpp pfqiknnved amgnymlnkf spsspesane
     1081 cskvlsdsal eapeatermt nvkssgstsv rkgplpflin ramscpsgep hastgregrk
     1141 kpltsgmdas eltpraweri ispvesdssv rdcsltkrqh qkenfqeyte kegkmaasrr
     1201 svfalsnedp lpfcsdlsgk ergktlhkvk ttstfsvsgd ednvkclevv siyytlprkp
     1261 skkfcnllqq ytqntnllie spqvetetfp nalekdkqny streqsgtps cenlkmsvns
     1321 dqtlttenmt afrlsnrgpl aptlqemasv eaavslpeee skareifsdn laktplgdse
     1381 nkkergkklq setlhtslml qrknvseeks encqqsinss nsgpsslpal sevnignsqt
     1441 rrsswectgs graipftgsg kcpqkdhtst avgdgssgsq pregrgdigt ncqkmtnktl
     1501 shsesqvfal tpalhklqlg eetqsdepnl eslqseprel pqrsqeanmt esrkaedemq
     1561 ksawdqpslp egnknktnld dlvkgenrss vkhrlaamsk asrkfpakdv sprrhvatif
     1621 pqsgsrsgfd hlslgtvecn plfpeptpks aesigesrls engkhvkkse nllpitvlpn
     1681 repsthvsnq ksnsisqrhq nefknvsesp skhenskdvt aaqnlvresg apspitftsl
     1741 reaefsdnqr rlsppfplep aqksrvsspl asflqqqrsa sslewepeph lyrskslksi
     1801 nvhgdllrks hppkvrerhf sestsidnal srltlgnefs vnngysrrfr sfselpscdg
     1861 neswayrsgt ktgprsaisi yrpidygifg keqqlaflen vkrsltqgrl wkpsflknpg
     1921 flkddlrnpp npseslssns pssqvpedgl spseplniye ddpvdsdcdt dtttddeyyl
     1981 dendkesel
//
