ID   F1711_XENLA             Reviewed;         859 AA.
AC   Q5RJX2;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 56.
DE   RecName: Full=Protein FAM171A1;
DE   Flags: Precursor;
GN   Name=fam171a1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May be involved in the regulation of the cytoskeletal
CC       dynamics, plays a role in actin stress fiber formation.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC086468; AAH86468.1; -; mRNA.
DR   RefSeq; NP_001088656.1; NM_001095187.1.
DR   AlphaFoldDB; Q5RJX2; -.
DR   DNASU; 495830; -.
DR   GeneID; 495830; -.
DR   KEGG; xla:495830; -.
DR   CTD; 495830; -.
DR   Xenbase; XB-GENE-5725449; fam171a1.L.
DR   OMA; SWGHVQR; -.
DR   OrthoDB; 168316at2759; -.
DR   Proteomes; UP000186698; Chromosome 6L.
DR   Bgee; 495830; Expressed in internal ear and 19 other tissues.
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; Reference proteome; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..859
FT                   /note="Protein FAM171A1"
FT                   /id="PRO_0000274265"
FT   TOPO_DOM        21..307
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        308..328
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        329..859
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          397..421
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          484..509
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          771..859
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        402..416
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        484..498
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        796..827
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        828..859
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        163
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        194
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        198
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   859 AA;  94974 MW;  8886162A527762BF CRC64;
     MSGSTAVALL FCVLSCSVWG AGSKASHEHN AAAAAQDVTL KVQVSDVSTH QPIADAVIEI
     FANQVSAASG TTGADGTALV KLQYKLGSQL IVTATKQAYV PNSAPWRPLR LPVFSSLSLG
     LLPERSATLM VYDDIVQIVS GFQGSRLQPR VHFQRRALNL PGNATYKDLA AFLTAASTPW
     EIDSFPYLQG SDGNSTGNNS RFDLTPVTAV SFHLLNSDGT DIPVNGPIYV TVPLPTHSSL
     KHNAHVPAWR FDQKHGTWLK SSIGIIQQEG SQLTWTYIAP QMGYWVAAMS PSHPDPVVTQ
     DITSYHTIFL LAILGGIAFI LLVLLCILLY YCRRKCLKPR QHHRKLQLST ALDCSKKDQA
     TSMSHINLIS PIHMEMLSSS GEADMHTPML KPSYNTSRDF GSREELLSHQ EEKSRMSLDN
     LTPSGTLRQV YNKSLDHILM KSRKSAEISE EYTSTMKDEY RRSYNSVICQ PLFESKDKDL
     LSSTNHVTAG SKPNIQEQMH PVPSAPEPEQ LIDRRSNECM MSRSVDHLER PTSFSRPGQL
     ICYNSVDQVN DSVYRNVLPT LVIPAHYVKL PGEHPFVSQQ LIVSAEQQFE IERLQAELSH
     AQQMQPPPLS AQAISQQHLQ DGEGVEWSTQ NAMMSESVSI PASLNDAAIA QMNGEVQLLT
     EKALMELGGG RPMPHPRAWF VSLDGRSNAH IRHSYIDLQR AGKNGSNDAS LDSGVDMNEP
     KLGRKLRGEK LSMLHSSMQH PTLQEHQQLN QVNVSDSTAY TQLVYLEDMD QSPSECGTAV
     CSPEDSRPFI EAPAKKSGSQ TPSLQEETIK RTTESSPLPL SSPEHEFNIN DDSGEDQGEN
     KKSPWQKREE RPLLAFNKK