CC85A_HUMAN
ID CC85A_HUMAN Reviewed; 553 AA.
AC Q96PX6;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Coiled-coil domain-containing protein 85A;
GN Name=CCDC85A; Synonyms=KIAA1912;
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 [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=11572484; DOI=10.1093/dnares/8.4.179;
RA Nagase T., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XXI. The
RT complete sequences of 60 new cDNA clones from brain which code for large
RT proteins.";
RL DNA Res. 8:179-187(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP FUNCTION, INTERACTION WITH ARVCF; CTNND1; CTNND2 AND PKP4, AND SUBCELLULAR
RP LOCATION.
RX PubMed=25009281; DOI=10.1091/mbc.e13-08-0492;
RA Markham N.O., Doll C.A., Dohn M.R., Miller R.K., Yu H., Coffey R.J.,
RA McCrea P.D., Gamse J.T., Reynolds A.B.;
RT "DIPA-family coiled-coils bind conserved isoform-specific head domain of
RT p120-catenin family: potential roles in hydrocephalus and heterotopia.";
RL Mol. Biol. Cell 25:2592-2603(2014).
CC -!- FUNCTION: May play a role in cell-cell adhesion and epithelium
CC development through its interaction with proteins of the beta-catenin
CC family. {ECO:0000305|PubMed:25009281}.
CC -!- SUBUNIT: May interact with ARVCF; CTNND1; CTNND2 AND PKP4.
CC {ECO:0000305|PubMed:25009281}.
CC -!- INTERACTION:
CC Q96PX6; Q8TDW5-2: SYTL5; NbExp=3; IntAct=EBI-7257229, EBI-12243980;
CC Q96PX6; Q05BL1: TP53BP2; NbExp=4; IntAct=EBI-7257229, EBI-11952721;
CC -!- SUBCELLULAR LOCATION: Cell junction, adherens junction
CC {ECO:0000269|PubMed:25009281}.
CC -!- SIMILARITY: Belongs to the CCDC85 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB67805.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB067499; BAB67805.1; ALT_INIT; mRNA.
DR EMBL; AC007743; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC007744; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS46290.1; -.
DR RefSeq; NP_001073902.1; NM_001080433.1.
DR AlphaFoldDB; Q96PX6; -.
DR SMR; Q96PX6; -.
DR BioGRID; 125361; 67.
DR IntAct; Q96PX6; 5.
DR MINT; Q96PX6; -.
DR STRING; 9606.ENSP00000384040; -.
DR iPTMnet; Q96PX6; -.
DR PhosphoSitePlus; Q96PX6; -.
DR BioMuta; CCDC85A; -.
DR DMDM; 296439418; -.
DR EPD; Q96PX6; -.
DR jPOST; Q96PX6; -.
DR MassIVE; Q96PX6; -.
DR PaxDb; Q96PX6; -.
DR PeptideAtlas; Q96PX6; -.
DR PRIDE; Q96PX6; -.
DR ProteomicsDB; 77782; -.
DR Antibodypedia; 50392; 32 antibodies from 12 providers.
DR DNASU; 114800; -.
DR Ensembl; ENST00000407595.3; ENSP00000384040.2; ENSG00000055813.6.
DR GeneID; 114800; -.
DR KEGG; hsa:114800; -.
DR MANE-Select; ENST00000407595.3; ENSP00000384040.2; NM_001080433.2; NP_001073902.1.
DR UCSC; uc002rzn.4; human.
DR CTD; 114800; -.
DR DisGeNET; 114800; -.
DR GeneCards; CCDC85A; -.
DR HGNC; HGNC:29400; CCDC85A.
DR HPA; ENSG00000055813; Tissue enhanced (brain).
DR neXtProt; NX_Q96PX6; -.
DR OpenTargets; ENSG00000055813; -.
DR PharmGKB; PA144596452; -.
DR VEuPathDB; HostDB:ENSG00000055813; -.
DR eggNOG; KOG3819; Eukaryota.
DR GeneTree; ENSGT00940000157361; -.
DR HOGENOM; CLU_028762_1_1_1; -.
DR InParanoid; Q96PX6; -.
DR OMA; EHHEKSC; -.
DR OrthoDB; 1393196at2759; -.
DR PhylomeDB; Q96PX6; -.
DR TreeFam; TF320243; -.
DR PathwayCommons; Q96PX6; -.
DR SignaLink; Q96PX6; -.
DR BioGRID-ORCS; 114800; 11 hits in 1069 CRISPR screens.
DR ChiTaRS; CCDC85A; human.
DR GenomeRNAi; 114800; -.
DR Pharos; Q96PX6; Tdark.
DR PRO; PR:Q96PX6; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q96PX6; protein.
DR Bgee; ENSG00000055813; Expressed in prefrontal cortex and 111 other tissues.
DR Genevisible; Q96PX6; HS.
DR GO; GO:0005912; C:adherens junction; IDA:UniProtKB.
DR InterPro; IPR019359; CCDC85.
DR PANTHER; PTHR13546; PTHR13546; 1.
DR Pfam; PF10226; CCDC85; 1.
PE 1: Evidence at protein level;
KW Cell junction; Coiled coil; Methylation; Reference proteome.
FT CHAIN 1..553
FT /note="Coiled-coil domain-containing protein 85A"
FT /id="PRO_0000271104"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 433..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 43..109
FT /evidence="ECO:0000255"
FT COILED 137..169
FT /evidence="ECO:0000255"
FT COILED 412..443
FT /evidence="ECO:0000255"
FT COMPBIAS 220..258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..290
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..337
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..370
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..458
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 541
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q5SP85"
FT CONFLICT 20
FT /note="P -> S (in Ref. 1; BAB67805)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 553 AA; 59976 MW; FE620905745A556A CRC64;
MSKAAGGAAA AAAAAESCSP APAGSSAAPP APVEDLSKVS DEELLQWSKE ELIRSLRRAE
AEKVSAMLDH SNLIREVNRR LQLHLGEIRG LKDINQKLQE DNQELRDLCC FLDDDRQKGK
RVSREWQRLG RYTAGVMHKE VALYLQKLKD LEVKQEEVVK ENMELKELCV LLDEEKGAGC
AGSRCSIDSQ ASLCQLTAST APYVRDVGDG SSTSSTGSTD SPDHHKHHAS SGSPEHLQKP
RSEGSPEHSK HRSASPEHPQ KPRACGTPDR PKALKGPSPE HHKPLCKGSP EQQRHPHPGS
SPETLPKHVL SGSPEHFQKH RSGSSPEHAR HSGGSPEHLQ KHALGGSLEH LPRARGTSPE
HLKQHYGGSP DHKHGGGSGG SGGSGGGSRE GTLRRQAQED GSPHHRNVYS GMNESTLSYV
RQLEARVRQL EEENRMLPQA SQNRRQPPTR NSSNMEKGWG SRARRVLQWW QGCRGIGRCL
PTLPGSFRLS SGADGSNSSP NSAASFSGHA TPSQQPEPVV HSLKVVWRKL GDAAGSCPGI
RQHLSGNQYK GPM
