ID A0A287DGH5_ICTTR Unreviewed; 1267 AA.
AC A0A287DGH5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=PTPRF interacting protein alpha 1 {ECO:0000313|Ensembl:ENSSTOP00000032612.1};
GN Name=PPFIA1 {ECO:0000313|Ensembl:ENSSTOP00000032612.1};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000032612.1, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000032612.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the liprin family. Liprin-alpha subfamily.
CC {ECO:0000256|ARBA:ARBA00007026}.
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DR EMBL; AGTP01072141; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01072142; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01072143; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A287DGH5; -.
DR STRING; 43179.ENSSTOP00000032612; -.
DR Ensembl; ENSSTOT00000038917.1; ENSSTOP00000032612.1; ENSSTOG00000002704.3.
DR eggNOG; KOG0249; Eukaryota.
DR GeneTree; ENSGT01050000244900; -.
DR InParanoid; A0A287DGH5; -.
DR OrthoDB; 2906732at2759; -.
DR Proteomes; UP000005215; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
DR GO; GO:1903077; P:negative regulation of protein localization to plasma membrane; IEA:Ensembl.
DR GO; GO:0051497; P:negative regulation of stress fiber assembly; IEA:Ensembl.
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; Transcription Factor, Ets-1; 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; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR PANTHER; PTHR12587; LAR INTERACTING PROTEIN LIP -RELATED PROTEIN; 1.
DR PANTHER; PTHR12587:SF15; LIPRIN-ALPHA-1; 1.
DR Pfam; PF00536; SAM_1; 1.
DR Pfam; PF07647; SAM_2; 1.
DR SMART; SM00454; SAM; 3.
DR SUPFAM; SSF47769; SAM/Pointed domain; 3.
DR PROSITE; PS50105; SAM_DOMAIN; 3.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000005215}.
FT DOMAIN 913..979
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 1035..1092
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 1116..1185
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 214..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 451..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 676..890
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1232..1267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 97..131
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 252..388
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 494..542
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 225..239
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 706..724
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 746..772
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 784..802
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 803..828
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 861..880
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1267 AA; 142614 MW; E475D79DD59E5890 CRC64;
MMCEVMPTIS EAEGPPGGGG SHGSGSPSQP DADSHFEQLM VSMLEERDRL LDTLRETQET
LALTQGKLHE VGHERDSLQR QLSTALPQEF AALTKELNVC REQLLEREEE IAELKAERNN
TRLLLEHLEC LVSRHERSLR MTVVKRQAQS PAGVSSEVEV LKALKSLFEH HKALDEKVRE
RLRVALERCS LLEEELGATH KELMILKEQN NQKKVAAGGV PDASHEQEST PSTNGKRSSD
GSSSHEEDLA KVIELQEVID KQSREQSQMK ERLATLSSHV VELEEDLDTA RKDLIKSEEM
NTKLQRDVRE AMAQKEDMEE RITTLEKRYL AAQREATSVH DLNDKLENEI ANKDSLHRQT
EDKNRQLQER LELAEQKLQQ TLRKAETLPE VEAELAQRVA ALSKSDPLSS GSSAAKEAKV
LELTSKLRKA EERHGNIEER LRQMEAQLEE KNQELQRARQ REKMNEEHNK RLSDTVDKLL
SESNERLQLH LKERMAALED KNSLLREVEN AKKQLEETQH DKDQLVLNIE ALRAELDQMR
LRGASLHHGR PHLGSVPDFR FPVADGHTDA YSTSAVLRRP QKGRLAALRD EPSKVQTLNE
QDWERAQQAS VLANVAQAFE SDLDVSDGED DRDTLLSSVD LLSPSGQADA QTLAMMLQEQ
LDAINKEIRL IQEEKENTEQ RAEEIESRVG SGSLDNLGRF RSMSSLPPYP ASSLAGSSPP
GSGRSTPRRV PHSPAREVDR LGVMTLPSDL RKHRRKLPAS REEVRDDKAT IKCETSPPSS
PRSLRLDRLH RGALHAASQE DVRDIRNSTG SQDGPVSNPS SSNSSQDSLH KAPKKKGIKS
SIGRLFGKKE KGRPGQTGKE PSGQAGVSET ENSSQDALGL SKLGGQAEKN RKLQKKHELL
EEARRQGLPF AQWDGPTVVV WLELWVGMPA WYVAACRANV KSGAIMSALS DTEIQREIGI
SNPLHRLKLR LAIQEIMSLT SPSAPPTSRT TTGNVWLTHE EMETLAATPH TEDEEGSWAQ
TLAYGDMNHE WIGNEWLPSL GLPQYRSYFM ECLVDARMLD HLTKKDLRGQ LKMVDSFHRN
SFQCGIMCLR RLNYDRKELE RKREESQNEI KDVLVWSNDR VIRWILSIGL KEYANNLIES
GVHGALLALD ETFDFNALAL LLQIPTQNPQ ARAVLEREFN NLLVMGTDRR FDEDDDKSFR
RAPSWRKKFR PKDIRGLAAG SAETLPANFR VTSSMSSPSM QPKKMQLDGS VSGAQRLDSA
TVRTYSC
//
