F1711_HUMAN
ID F1711_HUMAN Reviewed; 890 AA.
AC Q5VUB5; D3DRT9; Q32M49; Q8N4I0;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Protein FAM171A1 {ECO:0000305};
DE AltName: Full=Astroprincin {ECO:0000303|PubMed:30312582};
DE Short=APCN {ECO:0000303|PubMed:30312582};
DE Flags: Precursor;
GN Name=FAM171A1 {ECO:0000312|HGNC:HGNC:23522};
GN Synonyms=APCN {ECO:0000303|PubMed:30312582}, C10orf38;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
RA Attalla H., Karlsson L., Paetau A., Andersson L.C.;
RT "Cloning and expression profile of a novel gene isolated from DiGeorge
RT syndrome critical region on chromosome 10.";
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-465.
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-855, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-159.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-358; SER-360; SER-422;
RP SER-525 AND SER-849, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-371; SER-443 AND SER-849, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [9]
RP FUNCTION, TISSUE SPECIFICITY, GLYCOSYLATION AT ASN-159 AND ASN-194,
RP MUTAGENESIS OF SER-136; ASN-159; ASN-190 AND ASN-194, TOPOLOGY, SUBCELLULAR
RP LOCATION, AND INTERACTION WITH ADAM10; NSG1 AND OAZ1.
RX PubMed=30312582; DOI=10.1016/j.ajpath.2018.09.006;
RA Rasila T., Saavalainen O., Attalla H., Lankila P., Haglund C., Hoelttae E.,
RA Andersson L.C.;
RT "Astroprincin (FAM171A1, C10orf38): A Regulator of Human Cell Shape and
RT Invasive Growth.";
RL Am. J. Pathol. 189:177-189(2019).
CC -!- FUNCTION: Involved in the regulation of the cytoskeletal dynamics,
CC plays a role in actin stress fiber formation.
CC {ECO:0000269|PubMed:30312582}.
CC -!- SUBUNIT: Interacts with ADAM10, NSG1 and OAZ1.
CC {ECO:0000269|PubMed:30312582}.
CC -!- INTERACTION:
CC Q5VUB5; A6NK89: RASSF10; NbExp=3; IntAct=EBI-2682893, EBI-6912267;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:30312582};
CC Single-pass type I membrane protein {ECO:0000305|PubMed:30312582}.
CC -!- TISSUE SPECIFICITY: Expressed in heart, brain, liver, skeletal muscle,
CC kidney and pancreas (PubMed:30312582). In brain, expressed by glia,
CC pyramidal neurons and astrocytes (at protein level) (PubMed:30312582).
CC Highly expressed in placental trophoblasts (PubMed:30312582).
CC {ECO:0000269|PubMed:30312582}.
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; AY683003; AAV85904.1; -; mRNA.
DR EMBL; AL590365; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL139338; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL607028; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471072; EAW86237.1; -; Genomic_DNA.
DR EMBL; BC034232; AAH34232.1; -; mRNA.
DR EMBL; BC109302; AAI09303.1; -; mRNA.
DR EMBL; BC109303; AAI09304.1; -; mRNA.
DR CCDS; CCDS31154.1; -.
DR RefSeq; NP_001010924.1; NM_001010924.1.
DR AlphaFoldDB; Q5VUB5; -.
DR BioGRID; 128680; 56.
DR IntAct; Q5VUB5; 12.
DR MINT; Q5VUB5; -.
DR STRING; 9606.ENSP00000367356; -.
DR GlyGen; Q5VUB5; 4 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q5VUB5; -.
DR PhosphoSitePlus; Q5VUB5; -.
DR SwissPalm; Q5VUB5; -.
DR BioMuta; FAM171A1; -.
DR DMDM; 74747078; -.
DR EPD; Q5VUB5; -.
DR jPOST; Q5VUB5; -.
DR MassIVE; Q5VUB5; -.
DR MaxQB; Q5VUB5; -.
DR PaxDb; Q5VUB5; -.
DR PeptideAtlas; Q5VUB5; -.
DR PRIDE; Q5VUB5; -.
DR ProteomicsDB; 65405; -.
DR Antibodypedia; 25092; 67 antibodies from 15 providers.
DR DNASU; 221061; -.
DR Ensembl; ENST00000378116.9; ENSP00000367356.4; ENSG00000148468.17.
DR GeneID; 221061; -.
DR KEGG; hsa:221061; -.
DR MANE-Select; ENST00000378116.9; ENSP00000367356.4; NM_001010924.2; NP_001010924.1.
DR UCSC; uc001iob.4; human.
DR CTD; 221061; -.
DR DisGeNET; 221061; -.
DR GeneCards; FAM171A1; -.
DR HGNC; HGNC:23522; FAM171A1.
DR HPA; ENSG00000148468; Tissue enhanced (brain).
DR neXtProt; NX_Q5VUB5; -.
DR OpenTargets; ENSG00000148468; -.
DR PharmGKB; PA162387176; -.
DR VEuPathDB; HostDB:ENSG00000148468; -.
DR eggNOG; ENOG502QR89; Eukaryota.
DR GeneTree; ENSGT00950000183184; -.
DR HOGENOM; CLU_019729_0_0_1; -.
DR InParanoid; Q5VUB5; -.
DR OMA; SWGHVQR; -.
DR OrthoDB; 168316at2759; -.
DR PhylomeDB; Q5VUB5; -.
DR TreeFam; TF331338; -.
DR PathwayCommons; Q5VUB5; -.
DR SignaLink; Q5VUB5; -.
DR BioGRID-ORCS; 221061; 10 hits in 1081 CRISPR screens.
DR ChiTaRS; FAM171A1; human.
DR GenomeRNAi; 221061; -.
DR Pharos; Q5VUB5; Tdark.
DR PRO; PR:Q5VUB5; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q5VUB5; protein.
DR Bgee; ENSG00000148468; Expressed in inferior vagus X ganglion and 204 other tissues.
DR ExpressionAtlas; Q5VUB5; baseline and differential.
DR Genevisible; Q5VUB5; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; IMP:UniProtKB.
DR GO; GO:0043149; P:stress fiber assembly; IMP:UniProtKB.
DR InterPro; IPR018890; FAM171.
DR PANTHER; PTHR31626; PTHR31626; 1.
DR Pfam; PF10577; UPF0560; 1.
PE 1: Evidence at protein 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_0000274263"
FT TOPO_DOM 22..303
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:30312582"
FT TRANSMEM 304..324
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 325..890
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:30312582"
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:0007744|PubMed:23186163"
FT MOD_RES 360
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 371
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 422
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 443
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 525
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 849
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 855
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18318008"
FT CARBOHYD 159
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218,
FT ECO:0000269|PubMed:30312582"
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:0000269|PubMed:30312582"
FT VARIANT 465
FT /note="P -> S (in dbSNP:rs3814165)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_030220"
FT MUTAGEN 136
FT /note="S->A: No effect on glycosylation."
FT /evidence="ECO:0000269|PubMed:30312582"
FT MUTAGEN 159
FT /note="N->A: Decreases glycosylation levels. Abolishes
FT glycosylation; when associated with A-194."
FT /evidence="ECO:0000269|PubMed:30312582"
FT MUTAGEN 190
FT /note="N->A: No effect on glycosylation."
FT /evidence="ECO:0000269|PubMed:30312582"
FT MUTAGEN 194
FT /note="N->A: Decreases glycosylation levels. Abolishes
FT glycosylation; when associated with A-159."
FT /evidence="ECO:0000269|PubMed:30312582"
FT CONFLICT 118
FT /note="L -> P (in Ref. 4; AAI09304)"
FT /evidence="ECO:0000305"
FT CONFLICT 592
FT /note="G -> R (in Ref. 4; AAH34232)"
FT /evidence="ECO:0000305"
FT CONFLICT 670
FT /note="P -> Q (in Ref. 4; AAH34232)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 890 AA; 97854 MW; A0718E29A639FB72 CRC64;
MSRSATLLLC LLGCHVWKAV TKTLREPGAG AQEVTLKVHI SDASTHQPVA DALIEIFTNQ
ASIASGTSGT DGVAFIKFQY KLGSQLIVTA SKHAYVPNSA PWKPIRLPVF SSLSLGLLPE
RSATLMVYED VVQIVSGFQG ARPQPRVHFQ RRALRLPENT SYSDLTAFLT AASSPSEVDS
FPYLRGLDGN GTGNSTRHDL TPVTAVSVHL LSSNGTPVLV DGPIYVTVPL ATQSSLRHNA
YVAAWRFDQK LGTWLKSGLG LVHQEGSQLT WTYIAPQLGY WVAAMSPPIP GPVVTQDITT
YHTVFLLAIL GGMAFILLVL LCLLLYYCRR KCLKPRQHHR KLQLPAGLES SKRDQSTSMS
HINLLFSRRA SEFPGPLSVT SHGRPEAPGT KELMSGVHLE MMSPGGEGDL HTPMLKLSYS
TSQEFSSREE LLSCKEEDKS QISFDNLTPS GTLGKDYHKS VEVFPLKARK SMEREGYESS
GNDDYRGSYN TVLSQPLFEK QDREGPASTG SKLTIQEHLY PAPSSPEKEQ LLDRRPTECM
MSRSVDHLER PTSFPRPGQL 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
DAPSEPAASP HQRRSAHEEE EDDDDDDQGE DKKSPWQKRE ERPLMAFNIK
