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 08-MAY-2019, entry version 119. 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; 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., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., RA Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., RA Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., RA Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., RA Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., RA Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., RA Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., RA Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., RA Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., RA Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., RA Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., RA Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., RA Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., RA Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., RA Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., RA Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., RA Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., RA 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., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-855, AND IDENTIFICATION RP BY 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 RT enrichment and fractionation of phosphopeptides with strong anion RT exchange 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 RT multiple 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 RP SCALE 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 RP SER-849, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver 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, RP SUBCELLULAR 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., RA Hoelttae E., Andersson L.C.; RT "Astroprincin (FAM171A1, C10orf38): A Regulator of Human Cell Shape RT and 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 CC muscle, kidney and pancreas (PubMed:30312582). In brain, expressed CC by glia, pyramidal neurons and astrocytes (at protein level) CC (PubMed:30312582). Highly expressed in placental trophoblasts CC (PubMed:30312582). {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; 9. DR IntAct; Q5VUB5; 6. 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 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 H-InvDB; HIX0008675; -. 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; HOG000231925; -. DR InParanoid; Q5VUB5; -. DR OMA; EYRRSYN; -. DR OrthoDB; 168316at2759; -. DR PhylomeDB; Q5VUB5; -. DR TreeFam; TF331338; -. DR ChiTaRS; FAM171A1; human. DR GenomeRNAi; 221061; -. DR PRO; PR:Q5VUB5; -. DR Proteomes; UP000005640; Chromosome 10. DR Bgee; ENSG00000148468; Expressed in 239 organ(s), highest expression level in nucleus accumbens. 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; Complete proteome; Glycoprotein; Membrane; KW Phosphoprotein; Polymorphism; Reference proteome; Signal; KW Transmembrane; Transmembrane helix. FT SIGNAL 1 21 {ECO:0000255}. FT CHAIN 22 890 Protein FAM171A1. FT /FTId=PRO_0000274263. FT TOPO_DOM 22 303 Extracellular. FT {ECO:0000269|PubMed:30312582}. FT TRANSMEM 304 324 Helical. {ECO:0000255}. FT TOPO_DOM 325 890 Cytoplasmic. FT {ECO:0000269|PubMed:30312582}. FT MOD_RES 358 358 Phosphoserine. FT {ECO:0000244|PubMed:23186163}. FT MOD_RES 360 360 Phosphoserine. FT {ECO:0000244|PubMed:23186163}. FT MOD_RES 371 371 Phosphoserine. FT {ECO:0000244|PubMed:24275569}. FT MOD_RES 422 422 Phosphoserine. FT {ECO:0000244|PubMed:23186163}. FT MOD_RES 443 443 Phosphoserine. FT {ECO:0000244|PubMed:24275569}. FT MOD_RES 525 525 Phosphoserine. FT {ECO:0000244|PubMed:23186163}. FT MOD_RES 849 849 Phosphoserine. FT {ECO:0000244|PubMed:23186163, FT ECO:0000244|PubMed:24275569}. FT MOD_RES 855 855 Phosphoserine. FT {ECO:0000244|PubMed:18318008}. FT CARBOHYD 159 159 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:19159218, FT ECO:0000269|PubMed:30312582}. FT CARBOHYD 190 190 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 194 194 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:30312582}. FT VARIANT 465 465 P -> S (in dbSNP:rs3814165). FT {ECO:0000269|PubMed:15489334}. FT /FTId=VAR_030220. FT MUTAGEN 136 136 S->A: No effect on glycosylation. FT {ECO:0000269|PubMed:30312582}. FT MUTAGEN 159 159 N->A: Decreases glycosylation levels. FT Abolishes glycosylation; when associated FT with A-194. FT {ECO:0000269|PubMed:30312582}. FT MUTAGEN 190 190 N->A: No effect on glycosylation. FT {ECO:0000269|PubMed:30312582}. FT MUTAGEN 194 194 N->A: Decreases glycosylation levels. FT Abolishes glycosylation; when associated FT with A-159. FT {ECO:0000269|PubMed:30312582}. FT CONFLICT 118 118 L -> P (in Ref. 4; AAI09304). FT {ECO:0000305}. FT CONFLICT 592 592 G -> R (in Ref. 4; AAH34232). FT {ECO:0000305}. FT CONFLICT 670 670 P -> Q (in Ref. 4; AAH34232). FT {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 //