ID   RIM3C_HUMAN             Reviewed;        1639 AA.
AC   A6NJZ7;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2012, sequence version 3.
DT   27-MAR-2024, entry version 113.
DE   RecName: Full=RIMS-binding protein 3C;
DE            Short=RIM-BP3.C;
DE   AltName: Full=RIMS-binding protein 3.3;
DE            Short=RIM-BP3.3;
GN   Name=RIMBP3C;
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 GENOMIC DNA].
RX   PubMed=10591208; DOI=10.1038/990031;
RA   Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA   Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA   Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA   Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA   Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA   Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA   Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA   Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA   Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA   Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA   Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA   Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA   Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA   Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA   Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA   Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA   Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA   Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA   Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA   Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA   Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA   Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA   Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA   Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA   Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA   Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA   Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA   Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA   Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA   Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA   Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA   Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA   Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA   McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA   Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA   Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA   Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA   Wright H.;
RT   "The DNA sequence of human chromosome 22.";
RL   Nature 402:489-495(1999).
RN   [2]
RP   INTERACTION WITH FASLG.
RX   PubMed=19807924; DOI=10.1186/1471-2172-10-53;
RA   Voss M., Lettau M., Janssen O.;
RT   "Identification of SH3 domain interaction partners of human FasL (CD178) by
RT   phage display screening.";
RL   BMC Immunol. 10:53-53(2009).
CC   -!- FUNCTION: Probable component of the manchette, a microtubule-based
CC       structure which plays a key role in sperm head morphogenesis during
CC       late stages of sperm development. {ECO:0000250|UniProtKB:Q3V0F0}.
CC   -!- SUBUNIT: Interacts with LRGUK (via guanylate kinase-like domain).
CC       Interacts (via C-terminus) with HOOK1 (via coiled-coil region) (By
CC       similarity). May interact with FASLG (PubMed:19807924).
CC       {ECO:0000250|UniProtKB:Q3V0F0, ECO:0000269|PubMed:19807924}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000250|UniProtKB:Q3V0F0}.
CC   -!- SIMILARITY: Belongs to the RIMBP family. {ECO:0000305}.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-95 is the initiator.
CC       {ECO:0000305}.
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DR   EMBL; AP000557; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS46669.1; -.
DR   RefSeq; NP_001122105.1; NM_001128633.1.
DR   AlphaFoldDB; A6NJZ7; -.
DR   SMR; A6NJZ7; -.
DR   BioGRID; 127271; 17.
DR   IntAct; A6NJZ7; 1.
DR   STRING; 9606.ENSP00000390630; -.
DR   iPTMnet; A6NJZ7; -.
DR   PhosphoSitePlus; A6NJZ7; -.
DR   BioMuta; RIMBP3C; -.
DR   EPD; A6NJZ7; -.
DR   jPOST; A6NJZ7; -.
DR   MassIVE; A6NJZ7; -.
DR   MaxQB; A6NJZ7; -.
DR   PaxDb; 9606-ENSP00000390630; -.
DR   PeptideAtlas; A6NJZ7; -.
DR   ProteomicsDB; 1366; -.
DR   DNASU; 150221; -.
DR   Ensembl; ENST00000433039.2; ENSP00000390630.1; ENSG00000183246.8.
DR   GeneID; 150221; -.
DR   KEGG; hsa:150221; -.
DR   MANE-Select; ENST00000433039.2; ENSP00000390630.1; NM_001128633.2; NP_001122105.1.
DR   UCSC; uc002zuy.5; human.
DR   AGR; HGNC:33892; -.
DR   CTD; 150221; -.
DR   GeneCards; RIMBP3C; -.
DR   HGNC; HGNC:33892; RIMBP3C.
DR   HPA; ENSG00000183246; Tissue enriched (testis).
DR   MIM; 612701; gene.
DR   neXtProt; NX_A6NJZ7; -.
DR   OpenTargets; ENSG00000183246; -.
DR   VEuPathDB; HostDB:ENSG00000183246; -.
DR   eggNOG; KOG3632; Eukaryota.
DR   GeneTree; ENSGT00950000183203; -.
DR   HOGENOM; CLU_001979_2_1_1; -.
DR   InParanoid; A6NJZ7; -.
DR   OrthoDB; 5403222at2759; -.
DR   PhylomeDB; A6NJZ7; -.
DR   TreeFam; TF316230; -.
DR   PathwayCommons; A6NJZ7; -.
DR   SignaLink; A6NJZ7; -.
DR   SIGNOR; A6NJZ7; -.
DR   BioGRID-ORCS; 150221; 18 hits in 326 CRISPR screens.
DR   ChiTaRS; RIMBP3C; human.
DR   GenomeRNAi; 150221; -.
DR   Pharos; A6NJZ7; Tdark.
DR   PRO; PR:A6NJZ7; -.
DR   Proteomes; UP000005640; Chromosome 22.
DR   RNAct; A6NJZ7; Protein.
DR   Bgee; ENSG00000183246; Expressed in right testis and 23 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; IBA:GO_Central.
DR   GO; GO:0030156; F:benzodiazepine receptor binding; IBA:GO_Central.
DR   GO; GO:0009566; P:fertilization; IBA:GO_Central.
DR   GO; GO:0007286; P:spermatid development; IBA:GO_Central.
DR   CDD; cd00063; FN3; 1.
DR   CDD; cd11851; SH3_RIM-BP; 1.
DR   CDD; cd12014; SH3_RIM-BP_1; 1.
DR   CDD; cd22249; UDM1_RNF168_RNF169-like; 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; 2.
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.
DR   Genevisible; A6NJZ7; HS.
PE   1: Evidence at protein level;
KW   Coiled coil; Cytoplasm; Cytoskeleton; Differentiation; Reference proteome;
KW   Repeat; SH3 domain; Spermatogenesis.
FT   CHAIN           1..1639
FT                   /note="RIMS-binding protein 3C"
FT                   /id="PRO_0000332275"
FT   DOMAIN          832..899
FT                   /note="SH3 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   DOMAIN          995..1083
FT                   /note="Fibronectin type-III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          1088..1184
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          1452..1520
FT                   /note="SH3 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   DOMAIN          1569..1636
FT                   /note="SH3 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          215..240
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          295..364
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          697..811
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1251..1273
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1292..1325
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1392..1413
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          21..143
FT                   /evidence="ECO:0000255"
FT   COILED          409..442
FT                   /evidence="ECO:0000255"
FT   COILED          480..619
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        322..342
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        737..751
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        759..803
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1255..1273
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1392..1406
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1639 AA;  180950 MW;  A91AA22674EA0F26 CRC64;
     MAKDSPSPLG ASPKKPGCSS PAAAVLENQR RELEKLRAEL EAERAGWRAE RRRFAARERQ
     LREEAERERR QLADRLRSKW EAQRSRELRQ LQEEMQRERE AEIRQLLRWK EAEQRQLQQL
     LHRERDGVVR QARELQRQLA EELVNRGHCS RPGASEVSAA QCRCRLQEVL AQLRWQTDGE
     QAARIRYLQA ALEVERQLFL KYILAHFRGH PALSGSPDPQ AVHSLEEPLP QTSSGSCHAP
     KPACQLGSLD SLSAEVGVRS RSLGLVSSAC SSSPDGLLST HASSLDCFAP ACSRSLDSTR
     SLPKASKSEE RPSSPDTSTP GSRRLSPPPS PLPPPPPPSA HRKLSNPRGG EGSESQPCEV
     LTPSPPGLGH HELIKLNWLL AKALWVLARR CYTLQEENKQ LRRAGCPYQA DEKVKRLKVK
     RAELTGLARR LADRARELQE TNLRAVSAPI PGESCAGLEL CQVFARQRAR DLSEQASAPL
     AKDKQIEELR QECHLLQARV ASGPCSDLHT GRGGPCTQWL NVRDLDRLQR ESQREVLRLQ
     RQLMLQQGNG GAWPEAGGQS ATCEEVRRQM LALERELDQR RRECQELGTQ AAPARRRGEE
     AETQLQAALL KNAWLAEENG RLQAKTDWVR KVEAENSEVR GHLGRACQER DASGLIAEQL
     LQQAARGQDR QQQLQRDPQK ALCDLHPSWK EIQALQCRPG HPPEQPWETS QMPESQVKGS
     RRPKFHARPE DYAVSQPNRD IQEKREASLE ESPVALGESA SVPQVSETVP ASQPLSKKTS
     SQSNSSSEGS MWATVPSSPT LDRDTASEVD DLEPDSVSLA LEMGGSAAPA APKLKIFMAQ
     YNYNPFEGPN DHPEGELPLT AGDYIYIFGD MDEDGFYEGE LDDGRRGLVP SNFVEQIPDS
     YIPGCLPAKS PDLGPSQLPA GQDEALEEDS LLSGKAQGMV DRGLCQMVRV GSKTEVATEI
     LDTKTEACQL GLLQSMGKQG LSRPLLGTKG VLRMAPMQLH LQNVTATSAN ITWVYSSHRH
     PHVVYLDDRE HALTPAGVSC YTFQGLCPGT HYRVRVEVRL PWDLLQVYWG TMSSTVTFDT
     LLAGPPYPPL DVLVERHASP GVLVVSWLPV TIDSAGSSNG VQVTGYAVYA DGLKVCEVAD
     ATAGSTVLEF SQLQVPLTWQ KVSVRTMSLC GESLDSVPAQ IPEDFFMCHR WPETPPFSYT
     CGDPSTYRVT FPVCPQKLSL APPSAKASPH NPGSCGEPQA KFLEAFFEEP PRRQSPVSNL
     GSEGECPSSG AGSQAQELAE AWEGCRKDLL FQKSPQNHRP PSVSDQPGEK ENCYQHMGTS
     KSPAPGFIHL RTECGPRKEP CQEKAALERV LRQKQDAQGF TPPQLGASQQ YASDFHNVLK
     EEQEALCLDL RGTERREERR EPEPHSRQGQ ALGVKRGCQL HEPSSALCPA PSAKVIKMPR
     GGPQQLGTGA NTPARVFVAL SDYNPLVMSA NLKAAEEELV FQKRQLLRVW GSQDTHDFYL
     SECNRQVGNI PGRLVAEMEV GTEQTDRRWR SPAQGHLPSV AHLEDFQGLI IPQGSSLVLQ
     GNSKRLPLWT PKIMIAALDY DPGDGQMGGQ GKGRLALRAG DVVMVYGPMD DQGFYYGELG
     GHRGLVPAHL LDHMSLHGH
//