ID   FA8A1_HUMAN             Reviewed;         413 AA.
AC   Q9UBU6; B2R725;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 152.
DE   RecName: Full=Protein FAM8A1;
DE   AltName: Full=Autosomal highly conserved protein;
GN   Name=FAM8A1; Synonyms=AHCP;
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], AND TISSUE SPECIFICITY.
RX   PubMed=11707071; DOI=10.1006/geno.2001.6642;
RA   Jamain S., Girondot M., Leroy P., Clergue M., Quach H., Fellous M.,
RA   Bourgeron T.;
RT   "Transduction of the human gene FAM8A1 by endogenous retrovirus during
RT   primate evolution.";
RL   Genomics 78:38-45(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA   Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA   Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA   Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA   Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA   French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA   Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA   Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA   Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA   Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA   Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA   Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA   Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA   Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA   Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA   Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA   Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA   Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA   Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA   West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA   Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA   Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA   Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [4]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=15144186; DOI=10.1021/ac035352d;
RA   Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA   Peters E.C.;
RT   "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from
RT   human T cells using immobilized metal affinity chromatography and tandem
RT   mass spectrometry.";
RL   Anal. Chem. 76:2763-2772(2004).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT   kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-229, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-229, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and 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   [10]
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   [11]
RP   FUNCTION, IDENTIFICATION IN THE HRD1 COMPLEX, AND MUTAGENESIS OF
RP   120-TRP--TRP-122 AND TRP-131.
RX   PubMed=28827405; DOI=10.1242/jcs.206847;
RA   Schulz J., Avci D., Queisser M.A., Gutschmidt A., Dreher L.S., Fenech E.J.,
RA   Volkmar N., Hayashi Y., Hoppe T., Christianson J.C.;
RT   "Conserved cytoplasmic domains promote Hrd1 ubiquitin ligase complex
RT   formation for ER-associated degradation (ERAD).";
RL   J. Cell Sci. 130:3322-3335(2017).
CC   -!- FUNCTION: Plays a role in the assembly of the HRD1 complex, a complex
CC       involved in the ubiquitin-proteasome-dependent process of ER-associated
CC       degradation (ERAD). {ECO:0000269|PubMed:28827405}.
CC   -!- SUBUNIT: Component of the HRD1 complex, which comprises at least
CC       SYNV1/HRD1, FAM8A1, HERPUD1/HERP, OS9, SEL1L and UBE2J1. This
CC       interaction stabilizes FAM8A1 protein, preventing its proteasomal
CC       degradation. FAM8A1 binding to SYNV1 may promote recruitment of HERPUD1
CC       to the HRD1 complex. {ECO:0000269|PubMed:28827405}.
CC   -!- INTERACTION:
CC       Q9UBU6; Q86TM6: SYVN1; NbExp=20; IntAct=EBI-6309101, EBI-947849;
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed, with a higher level of
CC       expression in testis. {ECO:0000269|PubMed:11707071}.
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DR   EMBL; AF097027; AAF07850.1; -; mRNA.
DR   EMBL; AK312814; BAG35672.1; -; mRNA.
DR   EMBL; AL138824; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AF097026; AAF07849.1; -; Genomic_DNA.
DR   EMBL; CH471087; EAW55382.1; -; Genomic_DNA.
DR   EMBL; BC047881; AAH47881.1; -; mRNA.
DR   CCDS; CCDS4540.1; -.
DR   RefSeq; NP_057339.1; NM_016255.2.
DR   AlphaFoldDB; Q9UBU6; -.
DR   BioGRID; 119541; 96.
DR   CORUM; Q9UBU6; -.
DR   IntAct; Q9UBU6; 43.
DR   MINT; Q9UBU6; -.
DR   STRING; 9606.ENSP00000259963; -.
DR   TCDB; 2.A.133.1.4; the rdd na+(li+)(k+)/h+ antiporter (rdd) family.
DR   iPTMnet; Q9UBU6; -.
DR   PhosphoSitePlus; Q9UBU6; -.
DR   SwissPalm; Q9UBU6; -.
DR   BioMuta; FAM8A1; -.
DR   DMDM; 74753230; -.
DR   EPD; Q9UBU6; -.
DR   jPOST; Q9UBU6; -.
DR   MassIVE; Q9UBU6; -.
DR   MaxQB; Q9UBU6; -.
DR   PaxDb; 9606-ENSP00000259963; -.
DR   PeptideAtlas; Q9UBU6; -.
DR   ProteomicsDB; 84070; -.
DR   Pumba; Q9UBU6; -.
DR   Antibodypedia; 68212; 105 antibodies from 16 providers.
DR   DNASU; 51439; -.
DR   Ensembl; ENST00000259963.4; ENSP00000259963.3; ENSG00000137414.7.
DR   GeneID; 51439; -.
DR   KEGG; hsa:51439; -.
DR   MANE-Select; ENST00000259963.4; ENSP00000259963.3; NM_016255.3; NP_057339.1.
DR   UCSC; uc003ncc.4; human.
DR   AGR; HGNC:16372; -.
DR   CTD; 51439; -.
DR   DisGeNET; 51439; -.
DR   GeneCards; FAM8A1; -.
DR   HGNC; HGNC:16372; FAM8A1.
DR   HPA; ENSG00000137414; Low tissue specificity.
DR   MIM; 618409; gene.
DR   neXtProt; NX_Q9UBU6; -.
DR   OpenTargets; ENSG00000137414; -.
DR   PharmGKB; PA27986; -.
DR   VEuPathDB; HostDB:ENSG00000137414; -.
DR   eggNOG; KOG4647; Eukaryota.
DR   GeneTree; ENSGT00390000007346; -.
DR   HOGENOM; CLU_053631_1_0_1; -.
DR   InParanoid; Q9UBU6; -.
DR   OMA; QEQAGCE; -.
DR   OrthoDB; 2883352at2759; -.
DR   PhylomeDB; Q9UBU6; -.
DR   TreeFam; TF314024; -.
DR   PathwayCommons; Q9UBU6; -.
DR   SignaLink; Q9UBU6; -.
DR   SIGNOR; Q9UBU6; -.
DR   BioGRID-ORCS; 51439; 9 hits in 1156 CRISPR screens.
DR   GenomeRNAi; 51439; -.
DR   Pharos; Q9UBU6; Tbio.
DR   PRO; PR:Q9UBU6; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; Q9UBU6; Protein.
DR   Bgee; ENSG00000137414; Expressed in Brodmann (1909) area 23 and 211 other cell types or tissues.
DR   ExpressionAtlas; Q9UBU6; baseline and differential.
DR   GO; GO:0000836; C:Hrd1p ubiquitin ligase complex; IDA:FlyBase.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IC:FlyBase.
DR   InterPro; IPR039871; FAM8A1.
DR   InterPro; IPR010432; RDD.
DR   PANTHER; PTHR13659; AUTOSOMAL HIGHLY CONSERVED PROTEIN; 1.
DR   PANTHER; PTHR13659:SF5; PROTEIN FAM8A1; 1.
DR   Pfam; PF06271; RDD; 1.
DR   Genevisible; Q9UBU6; HS.
PE   1: Evidence at protein level;
KW   Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..413
FT                   /note="Protein FAM8A1"
FT                   /id="PRO_0000087167"
FT   TRANSMEM        257..277
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        304..324
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        371..391
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          242..408
FT                   /note="RDD"
FT   REGION          1..105
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          107..139
FT                   /note="Necessary and sufficient to interact with SYVN1"
FT                   /evidence="ECO:0000269|PubMed:28827405"
FT   REGION          217..236
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        30..50
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         229
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   MUTAGEN         120..122
FT                   /note="WLW->ALA: Decreased interaction with SYVN1 and
FT                   HERPUD1."
FT                   /evidence="ECO:0000269|PubMed:28827405"
FT   MUTAGEN         131
FT                   /note="W->A: Decreased interaction with HERPUD1; no effect
FT                   on interaction with SYVN1."
FT                   /evidence="ECO:0000269|PubMed:28827405"
SQ   SEQUENCE   413 AA;  44123 MW;  35B92497907CCD2E CRC64;
     MAEGPEEARG HPPGQDDGGG DHEPVPSLRG PPTTAVPCPR DDPQAEPQAP GRPTAPGLAA
     AAAADKLEPP RELRKRGEAA SGSGAELQEQ AGCEAPEAAA PRERPARLSA REYSRQVHEW
     LWQSYCGYLT WHSGLAAFPA YCSPQPSPQS FPSGGAAVPQ AAAPPPPQLG YYNPFYFLSP
     GAAGPDPRTA AGISTPAPVA GLGPRAPHVQ ASVRATPVTR VGSAAPSRSP SETGRQAGRE
     YVIPSLAHRF MAEMVDFFIL FFIKATIVLS IMHLSGIKDI SKFAMHYIIE EIDEDTSMED
     LQKMMVVALI YRLLVCFYEI ICIWGAGGAT PGKFLLGLRV VTCDTSVLIA PSRVLVIPSS
     NVSITTSTIR ALIKNFSIAS FFPAFITLLF FQHNRTAYDI VAGTIVVKRN GVR
//