LOCUS       NP_082991                873 aa            linear   ROD 04-JUN-2024
DEFINITION  F-BAR domain only protein 1 [Mus musculus].
ACCESSION   NP_082991
VERSION     NP_082991.3
DBSOURCE    REFSEQ: accession NM_028715.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 873)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 873)
  AUTHORS   Ritter,B., Murphy,S., Dokainish,H., Girard,M., Gudheti,M.V.,
            Kozlov,G., Halin,M., Philie,J., Jorgensen,E.M., Gehring,K. and
            McPherson,P.S.
  TITLE     NECAP 1 regulates AP-2 interactions to control vesicle size,
            number, and cargo during clathrin-mediated endocytosis
  JOURNAL   PLoS Biol 11 (10), e1001670 (2013)
   PUBMED   24130457
REFERENCE   3  (residues 1 to 873)
  AUTHORS   Umasankar,P.K., Sanker,S., Thieman,J.R., Chakraborty,S.,
            Wendland,B., Tsang,M. and Traub,L.M.
  TITLE     Distinct and separable activities of the endocytic clathrin-coat
            components Fcho1/2 and AP-2 in developmental patterning
  JOURNAL   Nat Cell Biol 14 (5), 488-501 (2012)
   PUBMED   22484487
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BY274600.1, AK137333.1, BU614854.1 and BY601220.1.
            
            On Aug 8, 2009 this sequence version replaced NP_082991.2.
            
            Transcript Variant: This variant (1) represents the shortest
            transcript and encodes the functional protein.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC032207.1, AK137333.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..873
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="8"
                     /map="8 34.43 cM"
     Protein         1..873
                     /product="F-BAR domain only protein 1"
                     /calculated_mol_wt=94991
     Region          1..275
                     /region_name="Mediates membrane-binding.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K285.2)"
     Region          10..270
                     /region_name="F-BAR_FCHO1"
                     /note="The F-BAR (FES-CIP4 Homology and
                     Bin/Amphiphysin/Rvs) domain of FCH domain Only 1 protein;
                     cd07674"
                     /db_xref="CDD:153358"
     Site            order(10,13..15,18..19,22,25,28..29,32..33,35..36,39..40,
                     43..44,47,50..51,54,57,61..62,65..67,71,74,78,81,134,138,
                     141..142,145,172,175..176,179,182,186,189..190,194,201,
                     204..205,208..209,211..212,215,219,222..223,226,229..230,
                     233..234,236..237,240,243..245,248..250,252..254,256..264,
                     266..270)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:153358"
     Site            order(21,24,31,38,49,53,56,111,114,136,144,150,167,170)
                     /site_type="other"
                     /note="putative membrane interaction site"
                     /db_xref="CDD:153358"
     Region          153..172
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K285.2)"
     Region          267..439
                     /region_name="Mediates interaction with the adaptor
                     protein complex AP-2. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K285.2)"
     Site            295
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O14526; propagated from
                     UniProtKB/Swiss-Prot (Q8K285.2)"
     Region          302..347
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K285.2)"
     Site            343
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O14526; propagated from
                     UniProtKB/Swiss-Prot (Q8K285.2)"
     Site            368
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O14526; propagated from
                     UniProtKB/Swiss-Prot (Q8K285.2)"
     Region          381..600
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K285.2)"
     Site            518
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q8K285.2)"
     Region          593..873
                     /region_name="Mediates interaction with AGFG1, CALM, DAB2,
                     EPS15, EPS15R, ITSN1 and clathrin. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K285.2)"
     Site            600
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O14526; propagated from
                     UniProtKB/Swiss-Prot (Q8K285.2)"
     Region          611..872
                     /region_name="AP_MHD_Cterm"
                     /note="C-terminal domain of adaptor protein (AP) complexes
                     medium mu subunits and its homologs (MHD); cl10970"
                     /db_xref="CDD:472082"
     Region          813..833
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K285.2)"
     CDS             1..873
                     /gene="Fcho1"
                     /gene_synonym="3322402E17Rik"
                     /coded_by="NM_028715.3:117..2738"
                     /db_xref="CCDS:CCDS52588.1"
                     /db_xref="GeneID:74015"
                     /db_xref="MGI:MGI:1921265"
ORIGIN      
        1 msyfgehfwg dknhgfevly hcvkqgpvat keladfirer anieetyska maklsklasn
       61 gtpmgtfapl wevfrvssdk lalchleltr klhdllkdvl rygeeqlkth kkckeevlgt
      121 vdavqmlsgv gqllpksren ylsrcmdler lrrentsqke mdkaetkskk aadslrrsvd
      181 kynsaradfe ikmldsalrf qameeahlqh mkallgsyah svedthvqig qvheefkqnv
      241 envtvdmllr kfaeskgtgr ekpgpldfda yssaalqeam krlrgakafr lpglsrrepr
      301 asvdflesds gvppevddeg ftvrpdisqn ngaepprfss sdsdfddeep rkfyvhikpa
      361 ptravacsse aaaaqlrata gslilppgpg gtmkrhssrd tsgkpqrprs aprtgscaek
      421 plaseeplsk slfgpplesa fdhddftgss slgftsspsp fsssspenve dsgldspsha
      481 apgpspeswv prpgtpqspp tcraqhpepr glmprapspg pwgpeggads ltpadptreg
      541 laatlrrprs rkvscpltrs ngdlcrslsp splgssapti ppdrpsfstq mghgisrgps
      601 pvvlgsqdal pvatafteyv hayfrghsps clarvtgelt mtfpagivrv fsgtppppvl
      661 sfrlvntapv ehfqpnadli fsdpsqsdpe tkdfwlnmaa ltealqhqae qnptasyynl
      721 vllryqfsrp gpesvplqms ahwqcgptlt rvsveysyra gatavstplt nvqillpvge
      781 pvtsvrlqpa atwnteekrf twklpdvcea ggsghlsasw qpqsgpstps pvaaqftseg
      841 atlsgldlel lgggyrmslv krrfatgmyl vsc
//
