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Database: UniProt
Entry: RIMB3_MOUSE
LinkDB: RIMB3_MOUSE
Original site: RIMB3_MOUSE 
ID   RIMB3_MOUSE             Reviewed;        1606 AA.
AC   Q3V0F0; B9EJ89; E9PZY2; Q5DTW0;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2017, sequence version 2.
DT   24-JAN-2024, entry version 126.
DE   RecName: Full=RIMS-binding protein 3;
DE            Short=RIM-BP3;
GN   Name=Rimbp3; Synonyms=Gm603, Kiaa1666;
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] OF 91-1606.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 94-1606.
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 468-1606.
RC   TISSUE=Fetal brain;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT   complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT   screening of terminal sequences of cDNA clones randomly sampled from size-
RT   fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   FUNCTION, INTERACTION WITH HOOK1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP   DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX   PubMed=19091768; DOI=10.1242/dev.030858;
RA   Zhou J., Du Y.R., Qin W.H., Hu Y.G., Huang Y.N., Bao L., Han D.,
RA   Mansouri A., Xu G.L.;
RT   "RIM-BP3 is a manchette-associated protein essential for spermiogenesis.";
RL   Development 136:373-382(2009).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263 AND SER-274, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Testis;
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   [7]
RP   FUNCTION, INTERACTION WITH LRGUK, AND SUBCELLULAR LOCATION.
RX   PubMed=28003339; DOI=10.1096/fj.201600909r;
RA   Okuda H., DeBoer K., O'Connor A.E., Merriner D.J., Jamsai D., O'Bryan M.K.;
RT   "LRGUK1 is part of a multiprotein complex required for manchette function
RT   and male fertility.";
RL   FASEB J. 31:1141-1152(2017).
CC   -!- FUNCTION: Component of the manchette, a microtubule-based structure
CC       which plays a key role in sperm head morphogenesis during late stages
CC       of sperm development (PubMed:19091768, PubMed:28003339). Important for
CC       male fertility (PubMed:19091768). {ECO:0000269|PubMed:19091768,
CC       ECO:0000269|PubMed:28003339}.
CC   -!- SUBUNIT: Interacts with FASLG (By similarity). Interacts with LRGUK
CC       (via guanylate kinase-like domain) (PubMed:28003339). Interacts (via C-
CC       terminus) with HOOK1 (via coiled-coil region) (PubMed:19091768).
CC       {ECO:0000250|UniProtKB:A6NJZ7, ECO:0000269|PubMed:19091768,
CC       ECO:0000269|PubMed:28003339}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000269|PubMed:19091768, ECO:0000269|PubMed:28003339}. Note=In
CC       elongating spermatids, localizes to the manchette.
CC       {ECO:0000269|PubMed:19091768, ECO:0000269|PubMed:28003339}.
CC   -!- TISSUE SPECIFICITY: Specifically expressed in testis, where it
CC       localizes to postmeiotic germ cells (at protein level).
CC       {ECO:0000269|PubMed:19091768}.
CC   -!- DEVELOPMENTAL STAGE: Detected in testis from postnatal day 20 onwards
CC       (at protein level). In developing spermatozoa, weakly expressed in
CC       pachytene spermatocytes and round spermatids, and highly expressed in
CC       elongating spermatids (at protein level). Detected in residual bodies
CC       but not mature sperm (at protein level). {ECO:0000269|PubMed:19091768}.
CC   -!- DISRUPTION PHENOTYPE: Males are almost completely infertile, but
CC       otherwise have no visible phenotype. Sperm morphology is highly
CC       abnormal with deformed nuclei, detached acrosomes and an expanded
CC       perinuclear space. Defects are first apparent from the round spermatid
CC       stage and are associated with abnormal development of the manchette.
CC       {ECO:0000269|PubMed:19091768}.
CC   -!- SIMILARITY: Belongs to the RIMBP family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI41387.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAE21554.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AC154667; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK133200; BAE21554.1; ALT_INIT; mRNA.
DR   EMBL; BC141386; AAI41387.1; ALT_INIT; mRNA.
DR   EMBL; AK220410; BAD90457.1; -; mRNA.
DR   CCDS; CCDS27998.2; -.
DR   RefSeq; NP_001028510.2; NM_001033338.3.
DR   AlphaFoldDB; Q3V0F0; -.
DR   SMR; Q3V0F0; -.
DR   STRING; 10090.ENSMUSP00000127909; -.
DR   GlyGen; Q3V0F0; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q3V0F0; -.
DR   PhosphoSitePlus; Q3V0F0; -.
DR   SwissPalm; Q3V0F0; -.
DR   PaxDb; 10090-ENSMUSP00000127909; -.
DR   ProteomicsDB; 253287; -.
DR   Ensembl; ENSMUST00000169803.5; ENSMUSP00000127909.2; ENSMUSG00000071636.9.
DR   GeneID; 239731; -.
DR   KEGG; mmu:239731; -.
DR   AGR; MGI:2685449; -.
DR   CTD; 85376; -.
DR   MGI; MGI:2685449; Rimbp3.
DR   VEuPathDB; HostDB:ENSMUSG00000071636; -.
DR   eggNOG; KOG3632; Eukaryota.
DR   GeneTree; ENSGT00950000183203; -.
DR   InParanoid; Q3V0F0; -.
DR   OMA; CQAFARQ; -.
DR   OrthoDB; 5403222at2759; -.
DR   PhylomeDB; Q3V0F0; -.
DR   TreeFam; TF316230; -.
DR   BioGRID-ORCS; 239731; 0 hits in 79 CRISPR screens.
DR   ChiTaRS; Rimbp3; mouse.
DR   PRO; PR:Q3V0F0; -.
DR   Proteomes; UP000000589; Chromosome 16.
DR   RNAct; Q3V0F0; Protein.
DR   Bgee; ENSMUSG00000071636; Expressed in seminiferous tubule of testis and 40 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0030156; F:benzodiazepine receptor binding; IBA:GO_Central.
DR   GO; GO:0009566; P:fertilization; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0007286; P:spermatid development; IMP:ParkinsonsUK-UCL.
DR   CDD; cd00063; FN3; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   Gene3D; 2.30.30.40; SH3 Domains; 3.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR040325; RIMBP1/2/3.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   PANTHER; PTHR14234; RIM BINDING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR14234:SF21; RIMS-BINDING PROTEIN 3A-RELATED; 1.
DR   Pfam; PF07653; SH3_2; 3.
DR   SMART; SM00060; FN3; 2.
DR   SMART; SM00326; SH3; 3.
DR   SUPFAM; SSF49265; Fibronectin type III; 1.
DR   SUPFAM; SSF50044; SH3-domain; 3.
DR   PROSITE; PS50853; FN3; 2.
DR   PROSITE; PS50002; SH3; 3.
PE   1: Evidence at protein level;
KW   Coiled coil; Cytoplasm; Cytoskeleton; Differentiation; Phosphoprotein;
KW   Reference proteome; Repeat; SH3 domain; Spermatogenesis.
FT   CHAIN           1..1606
FT                   /note="RIMS-binding protein 3"
FT                   /id="PRO_0000259598"
FT   DOMAIN          822..889
FT                   /note="SH3 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   DOMAIN          982..1070
FT                   /note="Fibronectin type-III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          1075..1171
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          1420..1488
FT                   /note="SH3 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   DOMAIN          1536..1603
FT                   /note="SH3 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          41..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          217..249
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          295..352
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          677..731
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          744..781
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1234..1255
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1364..1392
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          24..146
FT                   /evidence="ECO:0000255"
FT   COILED          352..431
FT                   /evidence="ECO:0000255"
FT   COILED          461..649
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        230..244
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        295..311
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        338..352
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        677..704
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        705..719
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        748..781
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1238..1254
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         263
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         274
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
SQ   SEQUENCE   1606 AA;  177278 MW;  DE272DBA3740F604 CRC64;
     MTKDSPTPLG GGRASPKKPS SPGPAAAVLE EQRRELEKLR AELEGERARG RSERRRFATQ
     TRQLRESAEQ ERQQLADHLR SKWEARRLRE LRQLQEEVQR EREAEIRQLL RWKEAEMRQL
     QQLLHQERDV VLRQARELQR QLAQELVNRG YCSRSGASEA SAAQCRCRLQ EVLALLRWET
     DGEQAARIRH LQAALDVERQ LFLKYILEHF RWQPALPGPA DPQATHSLEE PPLEAQSNTG
     GTPKPARRLG SLESLNTGVR VHSPNDLLPT RAGSLESLAT AHSCSLDNTL NCSQASESEV
     RAPATSASIP DTSSPQPPPQ LPSIHRKPND LQKESSENKP CEASTSSPPG LDYQELVRQN
     SELAEALQVL VRRCCDLREE NLHLRRKGFS EEAGEKVKWL KVKHAELTDL AQRLEDRARK
     LQETNLRAMS APVPGESLEG LDLSQVFTCQ RAQDLSEQAG ALQAKDLQIE ALRRECHLLQ
     ARIAADLGSS SHPEEGATCA QWCNISDLDR LQRESQREVL RLQRQLTLHQ SKAGAWADAG
     RPSTPSEITR HQVQALEREL GLQRRECEEL SVQAAAAERR YEETEAQLQA ALHKGARLSE
     ENARLQALAN WMKKMADENS NVSRQQSHTR QRQELEATSL LAEQLLQQEG YAQDRRQQLQ
     HYKNKALSDL RTSGKEMQGL QFQPGHPSET SETTQASESQ ARDSGRPTFK TKSEERVLPL
     PTRDIQPPAC LSQQENPVIV EEPAAGPQVS DRNSTSQSLD SKPQAKKTSS QSNSSSEVES
     MWATVPSCLS LDMDTASEVD DLEPDSMSTP LEMRSLEAPI IPKLKLFLAR SSYNPFEGPS
     EHCQGKLPLT AGDYVYVFGD MDEDGFYEGE LVNGQRGLVP SNLVEPISGS PILNHLFLKS
     PDIGPTALPA GHSKVLKKGS LLLGEVQERG LCQVGRVDSK TDMAAESLKT KTEACWLGLK
     SSLEEQSFSR PLLEAKGAFC LAPMELQLQN VTATSATITW ASGSNRYPHV VYLDDEEHIL
     TPSGVNHYTF QGLHPGTCYR VRVGVQLPRD LLQVLWETTS STLTFDTPLA GPPDPPLDVL
     VEHHASPGVL VVSWLPVTID SAGSSNGVQV TGYAVYVDGF KVTEVADATA GNTLLEFSQL
     QVPLSCQKVS VRTMSLYGES LDSVPAQIPE DFFSCCPFLG APPFNYTDGN PFPVCHQKLV
     QASLGAKSSP RGPGNCGEPQ AKFLEAFPEE HPRKHLSLSS LSSDGTNSQA QGPTEAWKGY
     EKDLSFQKSP QNHKPPLLFG QSGVEEGHAP HICISGSPAP GFVHLSSEIG HGKIRCWEKP
     GLEKALLQNQ YAPMVPPHQQ GSSQCQPADF HHVFEEKEAL CLDSQGTEKP EQRKNKSQNG
     QRQGTPGSKR ECSVLCPAPT NKVIKMTSGS PDQLETDANN PVRVFLALFD HSPLVISVNS
     EAAEEELAFQ KGQLLRVWGS LDLHGFYHGE CNGHLGKIPG HLVVEVEVGT QQTDGRWHLP
     AQGHLLSETQ REDLEGLTNS QGSYMPQGNS RTPTLWTPKT MVAALDYDPR DGRAGVQAKG
     KLVLRAGDVV TVYGPVDDKG FYYGEYGGHR GLVPAHLLDD LPVHGE
//
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