SO6C1_MOUSE
ID SO6C1_MOUSE Reviewed; 706 AA.
AC Q8C0X7; Q3V161; Q9D4B7;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Solute carrier organic anion transporter family member 6C1 {ECO:0000312|MGI:MGI:1921691};
GN Name=Slco6c1 {ECO:0000312|MGI:MGI:1921691};
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 {ECO:0000312|EMBL:BAC26482.1};
RN [1] {ECO:0000312|EMBL:BAC26482.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC26482.1};
RC TISSUE=Testis {ECO:0000312|EMBL:BAC26482.1};
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 [2] {ECO:0000312|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000312|Proteomes:UP000000589};
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 [3] {ECO:0000312|EMBL:AAI39067.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis {ECO:0000312|EMBL:AAI39067.1};
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] {ECO:0007744|PubMed:21183079}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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] {ECO:0000305}
RP STRUCTURE BY ELECTRON MICROSCOPY (2.9 ANGSTROMS) OF THE CATSPER COMPLEX,
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, TRANSMEMBRANE DOMAINS,
RP TOPOLOGY, AND GLYCOSYLATION AT ASN-535.
RX PubMed=34225353; DOI=10.1038/s41586-021-03742-6;
RA Lin S., Ke M., Zhang Y., Yan Z., Wu J.;
RT "Structure of a mammalian sperm cation channel complex.";
RL Nature 595:746-750(2021).
CC -!- FUNCTION: Auxiliary component of the CatSper complex, a complex
CC involved in sperm cell hyperactivation. {ECO:0000269|PubMed:34225353}.
CC -!- SUBUNIT: Component of the CatSper complex or CatSpermasome composed of
CC the core pore-forming members CATSPER1, CATSPER2, CATSPER3 and CATSPER4
CC as well as auxiliary members CATSPERB, CATSPERG2, CATSPERD, CATSPERE,
CC CATSPERZ, C2CD6/CATSPERT, SLCO6C1, TMEM249, TMEM262 and EFCAB9
CC (PubMed:34225353). HSPA1 may be an additional auxiliary complex member
CC (By similarity). The core complex members CATSPER1, CATSPER2, CATSPER3
CC and CATSPER4 form a heterotetrameric channel (PubMed:34225353). The
CC auxiliary CATSPERB, CATSPERG2, CATSPERD and CATSPERE subunits form a
CC pavilion-like structure over the pore which stabilizes the complex
CC through interactions with CATSPER4, CATSPER3, CATSPER1 and CATSPER2
CC respectively (PubMed:34225353). SLCO6C1 interacts with CATSPERE and
CC TMEM262/CATSPERH interacts with CATSPERB, further stabilizing the
CC complex (PubMed:34225353) (By similarity). C2CD6/CATSPERT interacts at
CC least with CATSPERD and is required for targeting the CatSper complex
CC in the flagellar membrane (Probable). {ECO:0000250|UniProtKB:Q91ZR5,
CC ECO:0000269|PubMed:34225353, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium, flagellum membrane
CC {ECO:0000305}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:34225353}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8C0X7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8C0X7-2; Sequence=VSP_061423;
CC -!- SIMILARITY: Belongs to the organo anion transporter (TC 2.A.60) family.
CC {ECO:0000305}.
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DR EMBL; AK029505; BAC26482.1; -; mRNA.
DR EMBL; AK016647; BAB30358.1; -; mRNA.
DR EMBL; AK132668; BAE21291.1; -; mRNA.
DR EMBL; AK161249; BAE36268.1; -; mRNA.
DR EMBL; BC139066; AAI39067.1; -; mRNA.
DR EMBL; BC139067; AAI39068.1; -; mRNA.
DR CCDS; CCDS35677.1; -. [Q8C0X7-1]
DR RefSeq; NP_083218.1; NM_028942.4.
DR PDB; 7EEB; EM; 2.90 A; L=1-706.
DR PDBsum; 7EEB; -.
DR AlphaFoldDB; Q8C0X7; -.
DR SMR; Q8C0X7; -.
DR STRING; 10090.ENSMUSP00000027569; -.
DR TCDB; 1.A.1.19.1; the voltage-gated ion channel (vic) superfamily.
DR iPTMnet; Q3V161; -.
DR PaxDb; Q8C0X7; -.
DR PRIDE; Q8C0X7; -.
DR ProteomicsDB; 335142; -.
DR ProteomicsDB; 336751; -.
DR DNASU; 74441; -.
DR Ensembl; ENSMUST00000027569; ENSMUSP00000027569; ENSMUSG00000026331. [Q8C0X7-1]
DR Ensembl; ENSMUST00000189547; ENSMUSP00000140791; ENSMUSG00000026331. [Q8C0X7-2]
DR GeneID; 74441; -.
DR KEGG; mmu:74441; -.
DR UCSC; uc007cff.1; mouse. [Q8C0X7-1]
DR UCSC; uc011wpv.1; mouse.
DR CTD; 74441; -.
DR MGI; MGI:1921691; Slco6c1.
DR VEuPathDB; HostDB:ENSMUSG00000026331; -.
DR eggNOG; KOG3626; Eukaryota.
DR GeneTree; ENSGT01050000244906; -.
DR HOGENOM; CLU_008954_2_1_1; -.
DR InParanoid; Q8C0X7; -.
DR OMA; SIELCME; -.
DR OrthoDB; 228564at2759; -.
DR PhylomeDB; Q8C0X7; -.
DR TreeFam; TF317540; -.
DR BioGRID-ORCS; 74441; 4 hits in 71 CRISPR screens.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8C0X7; protein.
DR Bgee; ENSMUSG00000026331; Expressed in spermatocyte and 3 other tissues.
DR ExpressionAtlas; Q8C0X7; baseline and differential.
DR GO; GO:0036128; C:CatSper complex; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-KW.
DR GO; GO:0008514; F:organic anion transmembrane transporter activity; ISO:MGI.
DR GO; GO:0015347; F:sodium-independent organic anion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015711; P:organic anion transport; ISO:MGI.
DR GO; GO:0043252; P:sodium-independent organic anion transport; IBA:GO_Central.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR002350; Kazal_dom.
DR InterPro; IPR036058; Kazal_dom_sf.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR004156; OATP.
DR PANTHER; PTHR11388; PTHR11388; 1.
DR Pfam; PF07648; Kazal_2; 1.
DR Pfam; PF03137; OATP; 1.
DR SUPFAM; SSF100895; SSF100895; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS51465; KAZAL_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Cell projection; Cilium;
KW Disulfide bond; Flagellum; Glycoprotein; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..706
FT /note="Solute carrier organic anion transporter family
FT member 6C1"
FT /id="PRO_0000454937"
FT TOPO_DOM 1..94
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:34225353"
FT TRANSMEM 95..118
FT /note="Helical; Name=1"
FT /evidence="ECO:0000269|PubMed:34225353"
FT TOPO_DOM 119..130
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:34225353"
FT TRANSMEM 131..151
FT /note="Helical; Name=2"
FT /evidence="ECO:0000269|PubMed:34225353"
FT TOPO_DOM 152..159
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:34225353"
FT TRANSMEM 160..180
FT /note="Helical; Name=3"
FT /evidence="ECO:0000269|PubMed:34225353"
FT TOPO_DOM 181..218
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:34225353"
FT TRANSMEM 219..241
FT /note="Helical; Name=4"
FT /evidence="ECO:0000269|PubMed:34225353"
FT TOPO_DOM 242..253
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:34225353"
FT TRANSMEM 254..277
FT /note="Helical; Name=5"
FT /evidence="ECO:0000269|PubMed:34225353"
FT TOPO_DOM 278..301
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:34225353"
FT TRANSMEM 302..324
FT /note="Helical; Name=6"
FT /evidence="ECO:0000269|PubMed:34225353"
FT TOPO_DOM 325..374
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:34225353"
FT TRANSMEM 375..396
FT /note="Helical; Name=7"
FT /evidence="ECO:0000269|PubMed:34225353"
FT TOPO_DOM 397..410
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:34225353"
FT TRANSMEM 411..432
FT /note="Helical; Name=8"
FT /evidence="ECO:0000269|PubMed:34225353"
FT TOPO_DOM 433..445
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:34225353"
FT TRANSMEM 446..466
FT /note="Helical; Name=9"
FT /evidence="ECO:0000269|PubMed:34225353"
FT TOPO_DOM 467..565
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:34225353"
FT TRANSMEM 566..589
FT /note="Helical; Name=10"
FT /evidence="ECO:0000269|PubMed:34225353"
FT TOPO_DOM 590..604
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:34225353"
FT TRANSMEM 605..624
FT /note="Helical; Name=11"
FT /evidence="ECO:0000269|PubMed:34225353"
FT TOPO_DOM 625..652
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:34225353"
FT TRANSMEM 653..675
FT /note="Helical; Name=12"
FT /evidence="ECO:0000269|PubMed:34225353"
FT TOPO_DOM 676..706
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:34225353"
FT DOMAIN 485..540
FT /note="Kazal-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 499..500
FT /note="Reactive bond"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT CARBOHYD 214
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 486
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 535
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:34225353"
FT DISULFID 491..521
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 497..517
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 506..538
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT VAR_SEQ 195..211
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_061423"
FT CONFLICT 224
FT /note="A -> G (in Ref. 1; BAE21291)"
FT /evidence="ECO:0000305"
FT HELIX 85..89
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 93..124
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 129..147
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 149..156
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 159..176
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 179..183
FT /evidence="ECO:0007829|PDB:7EEB"
FT TURN 184..186
FT /evidence="ECO:0007829|PDB:7EEB"
FT TURN 194..196
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:7EEB"
FT TURN 213..215
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 216..247
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 250..279
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 285..288
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 290..323
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 329..339
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 358..370
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 372..401
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 407..415
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 418..436
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 440..465
FT /evidence="ECO:0007829|PDB:7EEB"
FT TURN 477..480
FT /evidence="ECO:0007829|PDB:7EEB"
FT TURN 484..487
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 490..494
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 504..506
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 512..515
FT /evidence="ECO:0007829|PDB:7EEB"
FT TURN 516..520
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 521..523
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 531..536
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 549..551
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 555..558
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 566..594
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 598..601
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 602..613
FT /evidence="ECO:0007829|PDB:7EEB"
FT TURN 614..618
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 619..631
FT /evidence="ECO:0007829|PDB:7EEB"
FT TURN 637..640
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 646..648
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 653..688
FT /evidence="ECO:0007829|PDB:7EEB"
SQ SEQUENCE 706 AA; 78986 MW; ADC596A589429ECD CRC64;
MAHVRNKKSD DKKAMVVAKE DTNKSESEGV TKLQTYLKTI PIAKKKFAKL PKRKKSPTSA
ELLLIDPRYS ASKEGPLGLG PIVLPFVQRF NNIDGFMTLY VAAVLIHGAL FAVVDMTLNI
YQVQFSLTRT EWYLMDFSDY IASFVVAIII AHFGSKGNRT RWIAASCILM GLESMLFAFP
FFTYEIIIPG RQSIELCMEE NEKRNIICGN SVPNRSKCIY FHIAGQCIHG IAGMPIYILG
ITFIFDHIPT SSCGFYLAIG HSAYLIGYLL GMVGGLQNFQ PPPKEKTVEI EPAKVYQLLQ
SGWWKTFLII AAISFCVSFM MVCFPTSLPG AHKLRLAKRK EPPTIDRRLK DMKIQPHLKG
FLHNIWHILK NPLMLTQAIC KVSEYLTFNT SLYFLPHHLQ TQFLITPGIA SLLTGAFVLP
GGIIGHFLGG LIVDRLEMTN KNKLKFTLVT TVVSVGLFLL IFFVECQTTT FAGINEDYDG
YGQLGNLTAD CNEYCDCTTS LYTSICGRDE KEYFSPCFAG CKATKVSQTE KTYYNCSCIK
EGLAASDDEG QFIDAIAGTC DSDCLKLPLF FAFYFSATVF SNMCSIPVIS IILQSVPANF
TSLSLGVTYA IVKFVASVPA PLLFRLSSAI ACIYWDNNRC GGKERCWIYN KNILVYEFMG
IWMSSQLIIV LLNIYAIQIH DVVVHGEITE SKTTVKDVKE QKERKA
