ID   F1711_PONAB             Reviewed;         890 AA.
AC   Q5RD34;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 58.
DE   RecName: Full=Protein FAM171A1;
DE   Flags: Precursor;
GN   Name=FAM171A1;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the regulation of the cytoskeletal dynamics,
CC       plays a role in actin stress fiber formation.
CC       {ECO:0000250|UniProtKB:Q5VUB5}.
CC   -!- SUBUNIT: Interacts with ADAM10, NSG1 and OAZ1.
CC       {ECO:0000250|UniProtKB:Q5VUB5}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q5VUB5};
CC       Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q5VUB5}.
CC   -!- SIMILARITY: Belongs to the FAM171 family. {ECO:0000305}.
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DR   EMBL; CR858084; CAH90323.1; -; mRNA.
DR   RefSeq; NP_001125149.1; NM_001131677.2.
DR   AlphaFoldDB; Q5RD34; -.
DR   STRING; 9601.ENSPPYP00000002452; -.
DR   GeneID; 100172036; -.
DR   KEGG; pon:100172036; -.
DR   CTD; 221061; -.
DR   eggNOG; ENOG502QR89; Eukaryota.
DR   InParanoid; Q5RD34; -.
DR   OrthoDB; 168316at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB.
DR   GO; GO:0043149; P:stress fiber assembly; ISS:UniProtKB.
DR   InterPro; IPR018890; FAM171.
DR   PANTHER; PTHR31626; PTHR31626; 1.
DR   Pfam; PF10577; UPF0560; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Glycoprotein; Membrane; Phosphoprotein; Reference proteome;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..890
FT                   /note="Protein FAM171A1"
FT                   /id="PRO_0000274264"
FT   TOPO_DOM        22..303
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        304..324
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        325..890
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          730..759
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          818..890
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        823..837
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        870..890
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         358
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5VUB5"
FT   MOD_RES         360
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5VUB5"
FT   MOD_RES         371
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5VUB5"
FT   MOD_RES         422
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5VUB5"
FT   MOD_RES         443
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5VUB5"
FT   MOD_RES         525
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5VUB5"
FT   MOD_RES         849
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5VUB5"
FT   MOD_RES         855
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5VUB5"
FT   CARBOHYD        190
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        194
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   890 AA;  97971 MW;  1E23B61A5F196897 CRC64;
     MSRSAALLLC LLGCHVWKAV TKTLREPGAG AQEVTLKVHI SDASTHQPVA DALIEIFTNQ
     ASIASGTSGT DGVAFIKFQY KLGSQLIVTA SKHAYVPNSA PWKPIRLPVF SSLSLGLLPE
     RSATLMVYED VVQIVSGFQG ARPQPRVHFQ RRALRLPENT SYSDLTAFLT AASSPSEVDS
     FPYLRGLDGN GTGNSTRHDL TPVTAVSVHL LSSNGTPVLV DGPIYVTVPL ATQSSLRHNA
     YVTAWRFDQK LGTWLKSGLG LVHQEGSQLT WTYIAPQLGY WVAAMSPPIP GPVVTQDITT
     YHTVFLLAIL GGMAFILLVL LCLLLYYCRR KCMKPRQHHR KLQLPAGLES SKRDQSTSMS
     HINLLFSRRA SEFPGPLSVT SHGRPEAPGT KELMSGVHLE MMSPGGEGDL HTPMLKLSYS
     TSQEFSSREE LLSCKEEDKS QISFDNLTPS GTLRKDYHKS VEVFPLKARK SMEREGYESS
     GNDDYRGSYN TVLSQPLFEK QDREGPASTG SKLTIQEHLY PAPSSPEKEQ LLDRRPTECM
     MSRSVDHLER PTSFPQPGQL ICCSSVDQVN DSVYRKVLPA LVIPAHYMKL PGDHSYVSQP
     LVVPADQQLE IERLQAELSN PHAGIFPHPS SQIQPQPLSS QAISQQHLQD AGTREWSPQN
     ASMSESLSIP ASLNDAALAQ MNSEVQLLTE KALMELGGGK PLPHPRAWFV SLDGRSNAHV
     RHSYIDLQRA GRNGSNDASL DSGVDMNEPK SARKGRGDAL SLQQNYPPVQ EHQQKEPRAP
     DSTAYTQLVY LDDVEQSGSE CGTTVCTPED SALRCLLEGS SRRSGGQLPS LQEETTRRTA
     DAPSEPAVSP HQRRSAHEEE EDDDDDDQGE DKKSPWQKRE ERPLMAFNIK