ID   F175B_CAMFO             Reviewed;         471 AA.
AC   E2AB17;
DT   17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 1.
DT   25-MAY-2022, entry version 31.
DE   RecName: Full=BRISC complex subunit FAM175B {ECO:0000305};
DE   AltName: Full=BRISC complex subunit KIAA0157 homolog {ECO:0000305};
GN   ORFNames=EAG_01033 {ECO:0000312|EMBL:EFN69293.1};
OS   Camponotus floridanus (Florida carpenter ant).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Formicinae; Camponotus.
OX   NCBI_TaxID=104421;
RN   [1] {ECO:0000312|EMBL:EFN69293.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=20798317; DOI=10.1126/science.1192428;
RA   Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA   Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA   Wang J., Liebig J.;
RT   "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT   saltator.";
RL   Science 329:1068-1071(2010).
RN   [2] {ECO:0007744|PDB:5CW3, ECO:0007744|PDB:5CW4, ECO:0007744|PDB:5CW5}
RP   X-RAY CRYSTALLOGRAPHY (2.54 ANGSTROMS) OF 1-289 IN COMPLEX WITH BRCC3,
RP   IDENTIFICATION IN THE BRISC COMPLEX, INTERACTION WITH BRCC3, SUBUNIT, AND
RP   MUTAGENESIS OF ASN-177.
RX   PubMed=26344097; DOI=10.1016/j.molcel.2015.07.028;
RA   Zeqiraj E., Tian L., Piggott C.A., Pillon M.C., Duffy N.M.,
RA   Ceccarelli D.F., Keszei A.F., Lorenzen K., Kurinov I., Orlicky S.,
RA   Gish G.D., Heck A.J., Guarne A., Greenberg R.A., Sicheri F.;
RT   "Higher-order assembly of BRCC36-KIAA0157 is required for DUB activity and
RT   biological function.";
RL   Mol. Cell 59:970-983(2015).
CC   -!- FUNCTION: Component of the BRISC complex that specifically cleaves
CC       'Lys-63'-linked polyubiquitin, leaving the last ubiquitin chain
CC       attached to its substrates (PubMed:26344097). Does not have activity by
CC       itself, but the catalytic subunit BRCC3/BRCC36 needs to be associated
CC       into a heterotetramer with FAM175B for minimal in vitro activity
CC       (PubMed:26344097). May act as a central scaffold protein that assembles
CC       the various components of the BRISC complex and retains them in the
CC       cytoplasm (By similarity). Plays a role in regulating the onset of
CC       apoptosis via its role in modulating 'Lys-63'-linked ubiquitination of
CC       target proteins (By similarity). Required for normal mitotic spindle
CC       assembly and microtubule attachment to kinetochores via its role in
CC       deubiquitinating numa1 (By similarity). {ECO:0000250|UniProtKB:Q15018,
CC       ECO:0000250|UniProtKB:Q3TCJ1, ECO:0000269|PubMed:26344097}.
CC   -!- SUBUNIT: Component of the BRISC complex, at least composed of
CC       FAM175B/ABRO1, BRCC3/BRCC36, BABAM2 and BABAM1/NBA1. Within the
CC       complex, interacts directly with BRCC3/BRCC36. The heterodimer with
CC       BRCC3/BRCC36 assembles into a heterotetramer. The BRISC complex binds
CC       polyubiquitin. {ECO:0000269|PubMed:26344097}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q15018}. Nucleus
CC       {ECO:0000250|UniProtKB:Q15018}. Cytoplasm, cytoskeleton, spindle pole
CC       {ECO:0000250|UniProtKB:Q15018}. Cytoplasm, cytoskeleton
CC       {ECO:0000250|UniProtKB:Q15018}. Note=A minor proportion is detected in
CC       the nucleus. Translocates into the nucleus in response to DNA damage.
CC       Directly binds to microtubules and is detected at the minus end of K-
CC       fibers. {ECO:0000250|UniProtKB:Q15018}.
CC   -!- SIMILARITY: Belongs to the FAM175 family. Abro1 subfamily.
CC       {ECO:0000305}.
CC   -!- CAUTION: Expected to lack catalytic activity.
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DR   EMBL; GL438234; EFN69293.1; -; Genomic_DNA.
DR   RefSeq; XP_011254731.1; XM_011256429.2.
DR   RefSeq; XP_019882846.1; XM_020027287.1.
DR   PDB; 5CW3; X-ray; 2.55 A; B/D=1-289.
DR   PDB; 5CW4; X-ray; 2.54 A; B/D=1-289.
DR   PDB; 5CW5; X-ray; 2.74 A; B/D=1-289.
DR   PDBsum; 5CW3; -.
DR   PDBsum; 5CW4; -.
DR   PDBsum; 5CW5; -.
DR   AlphaFoldDB; E2AB17; -.
DR   SMR; E2AB17; -.
DR   STRING; 104421.E2AB17; -.
DR   GeneID; 105250379; -.
DR   KEGG; cfo:105250379; -.
DR   InParanoid; E2AB17; -.
DR   OMA; HKQFASH; -.
DR   OrthoDB; 954711at2759; -.
DR   Proteomes; UP000000311; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   InterPro; IPR023238; FAM175.
DR   InterPro; IPR037518; MPN.
DR   PANTHER; PTHR31728; PTHR31728; 1.
DR   PRINTS; PR02051; PROTEINF175.
DR   PROSITE; PS50249; MPN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell cycle; Cell division; Coiled coil; Cytoplasm;
KW   Cytoskeleton; Mitosis; Nucleus; Reference proteome;
KW   Ubl conjugation pathway.
FT   CHAIN           1..471
FT                   /note="BRISC complex subunit FAM175B"
FT                   /id="PRO_0000435529"
FT   DOMAIN          7..161
FT                   /note="MPN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   REGION          343..445
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          245..272
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        352..378
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         177
FT                   /note="N->R: Strongly reduces deubiquitination by the BRISC
FT                   complex."
FT                   /evidence="ECO:0000269|PubMed:26344097"
FT   STRAND          5..11
FT                   /evidence="ECO:0007829|PDB:5CW4"
FT   HELIX           12..24
FT                   /evidence="ECO:0007829|PDB:5CW4"
FT   STRAND          25..27
FT                   /evidence="ECO:0007829|PDB:5CW4"
FT   STRAND          29..41
FT                   /evidence="ECO:0007829|PDB:5CW4"
FT   STRAND          55..66
FT                   /evidence="ECO:0007829|PDB:5CW4"
FT   HELIX           69..71
FT                   /evidence="ECO:0007829|PDB:5CW4"
FT   STRAND          75..77
FT                   /evidence="ECO:0007829|PDB:5CW3"
FT   HELIX           82..89
FT                   /evidence="ECO:0007829|PDB:5CW4"
FT   HELIX           93..95
FT                   /evidence="ECO:0007829|PDB:5CW4"
FT   STRAND          96..105
FT                   /evidence="ECO:0007829|PDB:5CW4"
FT   HELIX           113..129
FT                   /evidence="ECO:0007829|PDB:5CW4"
FT   HELIX           134..136
FT                   /evidence="ECO:0007829|PDB:5CW3"
FT   STRAND          138..146
FT                   /evidence="ECO:0007829|PDB:5CW4"
FT   STRAND          152..162
FT                   /evidence="ECO:0007829|PDB:5CW4"
FT   STRAND          168..171
FT                   /evidence="ECO:0007829|PDB:5CW4"
FT   STRAND          173..176
FT                   /evidence="ECO:0007829|PDB:5CW4"
FT   HELIX           205..211
FT                   /evidence="ECO:0007829|PDB:5CW4"
FT   HELIX           224..270
FT                   /evidence="ECO:0007829|PDB:5CW4"
SQ   SEQUENCE   471 AA;  52574 MW;  A91CB24E699D2DC4 CRC64;
     MADSDLLVTI SGAALSLLFF ENVRSVGNQM GFLLGEALEF IVKTYTDSDN QVETVKIHIN
     VEAIVTCPLA DLLHDSTNHI NKEKLKDFVR DKSKQVIGWF CFRRNTTNLT LTLKDKLLHK
     QFASHFSGVN GCKEDFFLTC LLNASTSETS GTHKFRHVFL RHNKRGMFEP ISLKINNLGD
     DASRHDGSDY KPTPVRKSTR TPDSFTKLIE SLNLDVARID GLDSAMLIQK AAEHHLMSLI
     PKVCESDLEV AELEKQVHEL KIKIATQQLA KRLKINGENC DRISKASKDN CFSEKIDSSK
     KNEVRIGDDA CLQREHIPSC TQSVGPNNRT VCRNTAACIA KSAEKSRRAG RSNLQESGNQ
     QQETQNFFTN SRRSIPEIAT ESICQEGSEI SMGRGRGSGR GSHEFTPGMK KIRRTPGTSH
     MHSSRERSTT PPEQDFSDAE CPISSPVLRS YSQVTKKTNL DKCNSMAPLD I