CBLN4_HUMAN
ID CBLN4_HUMAN Reviewed; 201 AA.
AC Q9NTU7; A8K0S5;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Cerebellin-4;
DE AltName: Full=Cerebellin-like glycoprotein 1;
DE Flags: Precursor;
GN Name=CBLN4; Synonyms=CBLNL1; ORFNames=UNQ718/PRO1382;
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].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP PROTEIN SEQUENCE OF 28-42.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
CC -!- FUNCTION: Acts as a synaptic organizer in specific subsets of neurons
CC in the brain (By similarity). Essential for the formation and
CC maintenance of inhibitory GABAergic synapses (By similarity). Promotes
CC the development of dendrite-targeting inhibitory GABAergic synapses
CC made by somatostatin-positive interneurons (By similarity). May
CC contribute to the function of ventral medial habenula region of the
CC brain implicated in the regulation of anxiety-related behaviors (By
CC similarity). May play a role in CBLN3 export from the endoplasmic
CC reticulum and secretion (By similarity).
CC {ECO:0000250|UniProtKB:Q8BME9}.
CC -!- SUBUNIT: Homohexamer; disulfide-linked homotrimers. The trimers are
CC assembled via the globular C1q domains. The trimers associate via N-
CC terminal cysteine residues to form disulfide-linked hexamers (By
CC similarity). May form oligomers with CBLN1, CBLN2 and CBLN3 prior to
CC secretion (By similarity). Strongly interacts with DCC in a NTN1-
CC displaceable fashion (By similarity). Weakly binds to NRXN1 and NRXN2
CC long and short isoforms produced by alternative promoter usage.
CC Interaction with NRXN3 short isoform is hardly detectable; no
CC interaction at all with NRXN3 long isoform (By similarity).
CC {ECO:0000250|UniProtKB:Q8BME9, ECO:0000250|UniProtKB:Q9R171}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q8BME9}. Synapse
CC {ECO:0000250|UniProtKB:Q8BME9}. Note=Detected at GABAergic synapses.
CC {ECO:0000250|UniProtKB:Q8BME9}.
CC -!- PTM: Sialoglycoprotein. {ECO:0000250|UniProtKB:Q8BME9}.
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DR EMBL; AY358527; AAQ88891.1; -; mRNA.
DR EMBL; AK289640; BAF82329.1; -; mRNA.
DR EMBL; AL117383; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC050026; AAH50026.1; -; mRNA.
DR EMBL; BC069402; AAH69402.1; -; mRNA.
DR EMBL; BC069488; AAH69488.1; -; mRNA.
DR EMBL; BC069516; AAH69516.1; -; mRNA.
DR CCDS; CCDS13448.1; -.
DR RefSeq; NP_542184.1; NM_080617.5.
DR AlphaFoldDB; Q9NTU7; -.
DR SMR; Q9NTU7; -.
DR BioGRID; 126652; 138.
DR IntAct; Q9NTU7; 16.
DR MINT; Q9NTU7; -.
DR STRING; 9606.ENSP00000064571; -.
DR GlyConnect; 2027; 2 N-Linked glycans (1 site).
DR GlyGen; Q9NTU7; 2 sites, 4 N-linked glycans (1 site).
DR PhosphoSitePlus; Q9NTU7; -.
DR BioMuta; CBLN4; -.
DR DMDM; 13626170; -.
DR MassIVE; Q9NTU7; -.
DR PaxDb; Q9NTU7; -.
DR PeptideAtlas; Q9NTU7; -.
DR PRIDE; Q9NTU7; -.
DR ProteomicsDB; 82632; -.
DR Antibodypedia; 28817; 114 antibodies from 27 providers.
DR DNASU; 140689; -.
DR Ensembl; ENST00000064571.3; ENSP00000064571.2; ENSG00000054803.4.
DR GeneID; 140689; -.
DR KEGG; hsa:140689; -.
DR MANE-Select; ENST00000064571.3; ENSP00000064571.2; NM_080617.6; NP_542184.1.
DR UCSC; uc002xxa.5; human.
DR CTD; 140689; -.
DR DisGeNET; 140689; -.
DR GeneCards; CBLN4; -.
DR HGNC; HGNC:16231; CBLN4.
DR HPA; ENSG00000054803; Group enriched (adrenal gland, brain, epididymis).
DR MIM; 615029; gene.
DR neXtProt; NX_Q9NTU7; -.
DR OpenTargets; ENSG00000054803; -.
DR PharmGKB; PA26120; -.
DR VEuPathDB; HostDB:ENSG00000054803; -.
DR eggNOG; ENOG502QV08; Eukaryota.
DR GeneTree; ENSGT00940000159728; -.
DR HOGENOM; CLU_001074_8_2_1; -.
DR InParanoid; Q9NTU7; -.
DR OMA; PTTDWKA; -.
DR OrthoDB; 1398761at2759; -.
DR PhylomeDB; Q9NTU7; -.
DR TreeFam; TF329591; -.
DR PathwayCommons; Q9NTU7; -.
DR SignaLink; Q9NTU7; -.
DR BioGRID-ORCS; 140689; 11 hits in 1063 CRISPR screens.
DR GenomeRNAi; 140689; -.
DR Pharos; Q9NTU7; Tbio.
DR PRO; PR:Q9NTU7; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q9NTU7; protein.
DR Bgee; ENSG00000054803; Expressed in secondary oocyte and 112 other tissues.
DR Genevisible; Q9NTU7; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0098982; C:GABA-ergic synapse; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:1904862; P:inhibitory synapse assembly; ISS:UniProtKB.
DR GO; GO:0099558; P:maintenance of synapse structure; IBA:GO_Central.
DR GO; GO:0009306; P:protein secretion; IEA:Ensembl.
DR Gene3D; 2.60.120.40; -; 1.
DR InterPro; IPR001073; C1q_dom.
DR InterPro; IPR008983; Tumour_necrosis_fac-like_dom.
DR Pfam; PF00386; C1q; 1.
DR PRINTS; PR00007; COMPLEMNTC1Q.
DR SMART; SM00110; C1Q; 1.
DR SUPFAM; SSF49842; SSF49842; 1.
DR PROSITE; PS50871; C1Q; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Reference proteome; Secreted; Sialic acid; Signal; Synapse.
FT SIGNAL 1..27
FT /evidence="ECO:0000269|PubMed:15340161"
FT CHAIN 28..201
FT /note="Cerebellin-4"
FT /id="PRO_0000003556"
FT DOMAIN 66..201
FT /note="C1q"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00368"
FT CARBOHYD 29
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 40
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:Q9R171"
FT DISULFID 44
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:Q9R171"
FT CONFLICT 191
FT /note="S -> P (in Ref. 2; BAF82329)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 201 AA; 21808 MW; 2CC9B6C25A1929B7 CRC64;
MGSGRRALSA VPAVLLVLTL PGLPVWAQND TEPIVLEGKC LVVCDSNPAT DSKGSSSSPL
GISVRAANSK VAFSAVRSTN HEPSEMSNKT RIIYFDQILV NVGNFFTLES VFVAPRKGIY
SFSFHVIKVY QSQTIQVNLM LNGKPVISAF AGDKDVTREA ATNGVLLYLD KEDKVYLKLE
KGNLVGGWQY STFSGFLVFP L
