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 26-FEB-2020, entry version 124. 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 -!- 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 SMR; Q5VUB5; -. DR BioGrid; 128680; 10. DR IntAct; Q5VUB5; 9. DR STRING; 9606.ENSP00000367356; -. 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 Ensembl; ENST00000378116; ENSP00000367356; ENSG00000148468. DR GeneID; 221061; -. DR KEGG; hsa:221061; -. DR UCSC; uc001iob.4; human. DR CTD; 221061; -. DR DisGeNET; 221061; -. DR GeneCards; FAM171A1; -. DR HGNC; HGNC:23522; FAM171A1. DR HPA; HPA051345; -. DR neXtProt; NX_Q5VUB5; -. DR OpenTargets; ENSG00000148468; -. DR PharmGKB; PA162387176; -. DR eggNOG; ENOG410IKM3; Eukaryota. DR eggNOG; ENOG410ZV9V; LUCA. DR GeneTree; ENSGT00950000183184; -. DR HOGENOM; CLU_019729_0_0_1; -. DR InParanoid; Q5VUB5; -. DR OMA; GEADMHT; -. DR OrthoDB; 168316at2759; -. DR PhylomeDB; Q5VUB5; -. DR TreeFam; TF331338; -. 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 nucleus accumbens and 238 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; Uncharacterised_FAM171. DR PANTHER; PTHR31626; PTHR31626; 1. DR Pfam; PF10577; UPF0560; 1. PE 1: Evidence at protein level; KW Cell membrane; Glycoprotein; Membrane; Phosphoprotein; Polymorphism; KW Reference proteome; 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 MOD_RES 358 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:23186163" FT MOD_RES 360 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:23186163" FT MOD_RES 371 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:24275569" FT MOD_RES 422 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:23186163" FT MOD_RES 443 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:24275569" FT MOD_RES 525 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:23186163" FT MOD_RES 849 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:23186163, FT ECO:0000244|PubMed:24275569" FT MOD_RES 855 FT /note="Phosphoserine" FT /evidence="ECO:0000244|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 //