CC88B_MOUSE
ID CC88B_MOUSE Reviewed; 1481 AA.
AC Q4QRL3; B2RX63;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Coiled-coil domain-containing protein 88B;
DE AltName: Full=Gipie {ECO:0000303|PubMed:21289099};
DE AltName: Full=Hook-related protein 3;
DE Short=HkRP3;
GN Name=Ccdc88b; Synonyms=Ccdc88;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 348-1481 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Eye;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-441, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-649; SER-1353 AND SER-1384,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP FUNCTION, INTERACTION WITH HSPA5, AND TISSUE SPECIFICITY.
RX PubMed=21289099; DOI=10.1091/mbc.e10-08-0724;
RA Matsushita E., Asai N., Enomoto A., Kawamoto Y., Kato T., Mii S., Maeda K.,
RA Shibata R., Hattori S., Hagikura M., Takahashi K., Sokabe M., Murakumo Y.,
RA Murohara T., Takahashi M.;
RT "Protective role of Gipie, a Girdin family protein, in endoplasmic
RT reticulum stress responses in endothelial cells.";
RL Mol. Biol. Cell 22:736-747(2011).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=25403443; DOI=10.1084/jem.20140455;
RA Kennedy J.M., Fodil N., Torre S., Bongfen S.E., Olivier J.F., Leung V.,
RA Langlais D., Meunier C., Berghout J., Langat P., Schwartzentruber J.,
RA Majewski J., Lathrop M., Vidal S.M., Gros P.;
RT "CCDC88B is a novel regulator of maturation and effector functions of T
RT cells during pathological inflammation.";
RL J. Exp. Med. 211:2519-2535(2014).
CC -!- FUNCTION: Acts as a positive regulator of T-cell maturation and
CC inflammatory function. Required for several functions of T-cells in
CC both the CD4(+) and the CD8(+) compartments and this includes
CC expression of cell surface markers of activation, proliferation, and
CC cytokine production in response to specific or non-specific stimulation
CC and during the course of infection with the mouse malaria parasite
CC Plasmodium berghei (PubMed:25403443). Enhances NK cell cytotoxicity by
CC positively regulating polarization of microtubule-organizing center
CC (MTOC) to cytotoxic synapse, lytic granule transport along
CC microtubules, and dynein-mediated clustering to MTOC (By similarity).
CC Interacts with HSPA5 and stabilizes the interaction between HSPA5 and
CC ERN1, leading to suppression of ERN1-induced JNK activation and
CC endoplasmic reticulum stress-induced apoptosis (PubMed:21289099).
CC {ECO:0000250|UniProtKB:A6NC98, ECO:0000269|PubMed:21289099,
CC ECO:0000269|PubMed:25403443}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with DOCK8 (By
CC similarity). Interacts (via C-terminus) with intact microtubules (By
CC similarity). Interacts with dynein-dynactin motor complex (By
CC similarity). Interacts (via C-terminus) with HSPA5 (PubMed:21289099).
CC {ECO:0000250|UniProtKB:A6NC98, ECO:0000269|PubMed:21289099}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:25403443};
CC Peripheral membrane protein {ECO:0000305}. Cytoplasm, cytoskeleton,
CC microtubule organizing center {ECO:0000250|UniProtKB:A6NC98}.
CC Endoplasmic reticulum {ECO:0000250|UniProtKB:A6NC98}. Golgi apparatus
CC {ECO:0000250|UniProtKB:A6NC98}. Cytoplasm
CC {ECO:0000250|UniProtKB:A6NC98}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q4QRL3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q4QRL3-2; Sequence=VSP_030966;
CC -!- TISSUE SPECIFICITY: Abundantly expressed in immune cells, including
CC both CD4(+) and CD8(+) T-cells and in myeloid cells (at protein level)
CC (PubMed:25403443). Expressed in endothelium (at protein level)
CC (PubMed:21289099). Expressed specifically in spleen, bone marrow, lymph
CC nodes and thymus (PubMed:25403443). Expressed in liver and heart
CC (PubMed:21289099). {ECO:0000269|PubMed:21289099,
CC ECO:0000269|PubMed:25403443}.
CC -!- DISRUPTION PHENOTYPE: Mice show defects in T-cell functions including
CC impaired maturation, significantly reduced activation, reduced cell
CC division as well as impaired cytokine production in response to
CC specific or non-specific stimulation and during the course of infection
CC with the mouse malaria parasite Plasmodium berghei.
CC {ECO:0000269|PubMed:25403443}.
CC -!- SIMILARITY: Belongs to the CCDC88 family. {ECO:0000305}.
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DR EMBL; AC120557; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC076600; AAH76600.1; -; mRNA.
DR EMBL; BC151001; AAI51002.1; -; mRNA.
DR EMBL; BC151009; AAI51010.1; -; mRNA.
DR CCDS; CCDS37900.1; -. [Q4QRL3-1]
DR RefSeq; NP_001074760.1; NM_001081291.1. [Q4QRL3-1]
DR AlphaFoldDB; Q4QRL3; -.
DR SMR; Q4QRL3; -.
DR STRING; 10090.ENSMUSP00000109067; -.
DR iPTMnet; Q4QRL3; -.
DR PhosphoSitePlus; Q4QRL3; -.
DR CPTAC; non-CPTAC-3967; -.
DR EPD; Q4QRL3; -.
DR jPOST; Q4QRL3; -.
DR MaxQB; Q4QRL3; -.
DR PaxDb; Q4QRL3; -.
DR PRIDE; Q4QRL3; -.
DR ProteomicsDB; 283722; -. [Q4QRL3-1]
DR ProteomicsDB; 283723; -. [Q4QRL3-2]
DR Antibodypedia; 15381; 49 antibodies from 11 providers.
DR Ensembl; ENSMUST00000113440; ENSMUSP00000109067; ENSMUSG00000047810. [Q4QRL3-1]
DR GeneID; 78317; -.
DR KEGG; mmu:78317; -.
DR UCSC; uc008gjb.1; mouse. [Q4QRL3-1]
DR CTD; 283234; -.
DR MGI; MGI:1925567; Ccdc88b.
DR VEuPathDB; HostDB:ENSMUSG00000047810; -.
DR eggNOG; KOG4643; Eukaryota.
DR GeneTree; ENSGT00940000162048; -.
DR HOGENOM; CLU_002567_1_0_1; -.
DR InParanoid; Q4QRL3; -.
DR OMA; ADSCFHH; -.
DR OrthoDB; 59187at2759; -.
DR PhylomeDB; Q4QRL3; -.
DR TreeFam; TF320231; -.
DR BioGRID-ORCS; 78317; 5 hits in 72 CRISPR screens.
DR PRO; PR:Q4QRL3; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q4QRL3; protein.
DR Bgee; ENSMUSG00000047810; Expressed in granulocyte and 64 other tissues.
DR ExpressionAtlas; Q4QRL3; baseline and differential.
DR Genevisible; Q4QRL3; MM.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0051959; F:dynein light intermediate chain binding; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IBA:GO_Central.
DR GO; GO:0030705; P:cytoskeleton-dependent intracellular transport; IBA:GO_Central.
DR GO; GO:0042832; P:defense response to protozoan; IMP:UniProtKB.
DR GO; GO:0001819; P:positive regulation of cytokine production; IMP:UniProtKB.
DR GO; GO:0050870; P:positive regulation of T cell activation; IMP:UniProtKB.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; IMP:UniProtKB.
DR Gene3D; 1.10.418.10; -; 1.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR043936; HOOK_N.
DR Pfam; PF19047; HOOK_N; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW Endoplasmic reticulum; Golgi apparatus; Membrane; Phosphoprotein;
KW Reference proteome; Stress response.
FT CHAIN 1..1481
FT /note="Coiled-coil domain-containing protein 88B"
FT /id="PRO_0000317455"
FT REGION 430..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 494..731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1331..1481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 200..225
FT /evidence="ECO:0000255"
FT COILED 258..491
FT /evidence="ECO:0000255"
FT COILED 731..1308
FT /evidence="ECO:0000255"
FT COMPBIAS 515..529
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..555
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..588
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..695
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1404..1420
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1450..1469
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 441
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 649
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1353
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1384
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 349..359
FT /note="QAAEVFKGQLE -> DSWVKRVKIQQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030966"
SQ SEQUENCE 1481 AA; 166608 MW; 3229089E792598B8 CRC64;
MEGAKGPRLR GFLSGSLATW ALGLAGLVGE AEESAGGTEE EEEEEEEEGA LCTEKRFLRL
IDGALLLRVL GIIAPSSRGG LRMVRGRDGP AACRMWNLCH LWGRLRDFYQ EELQLLILSP
PPDLQTMGCD PFSEEAVDEL ESILRLLLGA SVQCEHRELF IRHIRGLSLD VQSELAGAIQ
EVTQPGAGVV LALAGPESGE LVAEELEMQL RSLTGMMSRL ARERDLGAQR LAELLLEREP
AHLLLPEAPA NASAEGVSHH LALQLTNAKA QLRRLRQEVE EKAEQLLDSQ AEVQGLEAEI
RRLRQETQAL SAQAKRAELY REEAEALRER AGRLPRLQEE LRRCREKLQA AEVFKGQLEE
ERVLSEALEA SKVLLEEQLE VARERSARLH ETQRENLLLR TRLGEAHADL DSLRHQLEQL
VEENVELELE LQRSLEPPPG SPGEASLPGA APSLQDEVRE AEAGRLRAVE RENRELRGQL
QMLQAQLGSQ HPLLEEQREN SRQPPVPNRD PATPSALHHS PQSPACQIGG EGSESLDLPS
PASYSDITRS PKCSQAPDSH PELESPLQMV SQDPQTSDQA LQESDPTVET HQCLEKSGHR
VPLQSPIVWD PPQGPEVRIE VQELLGETGS REAPQGELVH KAQVLKQESP KCRPRSAELT
LREPLKDQKA LDRELELSKQ QKETGRHEQR PKGLESKLGP QKPQQTSEGV PDAWSREEPT
PGETLVSAIP EEQALRDEVA QLRREVAGLE VKLQAQAQRL EARSAEALCL SEELAQARRT
EAEAHQEAEA QAREQARLRE AVDTASLELE AASREREALA EALAAAGRER RQWERDGPRL
RAQVEAAEQQ VQALESQVRC HLEEAEREHA EKQALREELE KAVLRGQELG DRLEHLQEEL
EQAALERQKF LQEQENQHQR YRHLEQRLEA ELQAASTSKE EALMELKARA LQLEEELIQL
RQYPVDLATG ARAGPRTVET QNGRLIEVER NNATLVAEKA ALQGQLQHLE GQLGSLQGRA
QELLLQSQRA QEHSSRLQAE KSMMEMQGQE LHRKLGVLEE EVRAARRAQE ETRGQQQALL
RDHEALVQLQ RRQETELEGL LVRHRDLKAN MRALELAHRE LQGRHEQLQA QRANVEAQEV
ALLAERERLM QDGHRQRGLE EELRRLQNEH ERAQMLLAEV SRERGELQGE RGELRSRLAR
LELERAQLEI QSQQLRESNQ QLDLSACRLT TQCELLTQLR SAQEEENRQL LAEVQALSRE
NRELLERSLE SRDHLHREQR EYLDQLNALR REKQKLVEKI MDQYRVLEPG PLPRTKKGSW
LADKVKRLIR PRREGALHGG PRLGADGAGS TESLGGPLET ELPEGREADG TGSSSPAPMR
RVQSSLCLGD ETLAGGQRRR LSSRFPGGRS SASFSPGDTP RQRFRQRRPG PLGAPSTHSK
GSGVEWDGSI KTLSEHEADD TREAFQEQKP EKQFLTPSLS Q
