FR1L4_MOUSE
ID FR1L4_MOUSE Reviewed; 1992 AA.
AC A3KGK3; B7ZCP2;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 3.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Fer-1-like protein 4;
GN Name=Fer1l4;
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 954-1992 (ISOFORM 2).
RC TISSUE=Urinary bladder;
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).
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A3KGK3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A3KGK3-2; Sequence=VSP_034990, VSP_034991;
CC -!- SEQUENCE CAUTION:
CC Sequence=AK035669; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=CAX15728.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL833786; CAX15728.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AK035669; -; NOT_ANNOTATED_CDS; mRNA.
DR AlphaFoldDB; A3KGK3; -.
DR STRING; 10090.ENSMUSP00000105240; -.
DR iPTMnet; A3KGK3; -.
DR PhosphoSitePlus; A3KGK3; -.
DR PaxDb; A3KGK3; -.
DR PRIDE; A3KGK3; -.
DR ProteomicsDB; 267513; -. [A3KGK3-1]
DR ProteomicsDB; 267514; -. [A3KGK3-2]
DR MGI; MGI:1921812; Fer1l4.
DR eggNOG; KOG1326; Eukaryota.
DR InParanoid; A3KGK3; -.
DR TreeFam; TF316871; -.
DR ChiTaRS; Fer1l4; mouse.
DR PRO; PR:A3KGK3; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; A3KGK3; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007009; P:plasma membrane organization; IBA:GO_Central.
DR CDD; cd08373; C2A_Ferlin; 1.
DR CDD; cd04011; C2B_Ferlin; 1.
DR CDD; cd04018; C2C_Ferlin; 1.
DR CDD; cd04017; C2D_Ferlin; 1.
DR CDD; cd04037; C2E_Ferlin; 1.
DR CDD; cd08374; C2F_Ferlin; 1.
DR Gene3D; 2.60.40.150; -; 6.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR037726; C2A_Ferlin.
DR InterPro; IPR037720; C2B_Ferlin.
DR InterPro; IPR037722; C2C_Ferlin.
DR InterPro; IPR037723; C2D_Ferlin.
DR InterPro; IPR037724; C2E_Ferlin.
DR InterPro; IPR037725; C2F_Ferlin.
DR InterPro; IPR030001; Fer1l4.
DR InterPro; IPR012968; FerIin_dom.
DR InterPro; IPR037721; Ferlin.
DR InterPro; IPR012561; Ferlin_B-domain.
DR InterPro; IPR032362; Ferlin_C.
DR PANTHER; PTHR12546; PTHR12546; 1.
DR PANTHER; PTHR12546:SF36; PTHR12546:SF36; 1.
DR Pfam; PF00168; C2; 5.
DR Pfam; PF08150; FerB; 1.
DR Pfam; PF08151; FerI; 1.
DR Pfam; PF16165; Ferlin_C; 1.
DR SMART; SM00239; C2; 5.
DR SMART; SM01201; FerB; 1.
DR SMART; SM01202; FerI; 1.
DR SUPFAM; SSF49562; SSF49562; 7.
DR PROSITE; PS50004; C2; 7.
PE 2: Evidence at transcript level;
KW Alternative splicing; Calcium; Membrane; Metal-binding; Reference proteome;
KW Repeat; Transmembrane; Transmembrane helix.
FT CHAIN 1..1992
FT /note="Fer-1-like protein 4"
FT /id="PRO_0000346423"
FT TOPO_DOM 1..1952
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1953..1973
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1974..1992
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 1..97
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 214..330
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 369..502
FT /note="C2 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 951..1078
FT /note="C2 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 1126..1250
FT /note="C2 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 1430..1549
FT /note="C2 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 1675..1824
FT /note="C2 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 554..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 661..686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 691..710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1245..1276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1322..1361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1862..1885
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..603
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 663..686
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1337..1361
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1464
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1464
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1470
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1519
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1519
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1521
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1521
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1527
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1795
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1798
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1801
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT VAR_SEQ 1898..1901
FT /note="GKVE -> VRSP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_034990"
FT VAR_SEQ 1902..1992
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_034991"
SQ SEQUENCE 1992 AA; 223891 MW; 83BC3E0201C480D3 CRC64;
MALTVCVRHL TGLPGTHDRQ VRLCFRGFTQ KTRKIHCGRE ADVGELFRWP HYGSPLAGES
LSVQVVNCSR VFSPRPLGTL VISLQQLQSA GHLVLREALV DERLRVSPIQ VELDLKYQPP
EGAAGTWAEE DFGTPIRDSL ELIIPNVGFQ DMEPGEAQLE RRAVALGRRL ARSLGTQDDE
ENELELEPEL EEEPDVEISG VVFSPLKSRA LGLPRGDPFK VCKAQDFQVG VTVLEAQKLV
GVNINPYVAV RVGDQRKVTA TLRGTNCPFY NEYFLFEFHE TRLHLQDLLL EITAFHSQTL
PFMATRIGTF RMDLGMALDQ PDGHFHQKWA PLHDPRDTRA GTKGFVKITL SVRARGDLPL
PPPPPCPGTS SDIEKNLLLP HGVQAERPWA RLRVRVYRAE GLPTVRTGLL GSLARALHDQ
NVLLDPYVRV SFLGQQGETS VRGEETAPKW NEQLSFVELF PPLTRSLRLQ LRDNAPLVDV
ALATHVLDLR QISNSGRAAG FNPTFGPAWV PLYGSLPSGR LRDDLQSLNE GLGEGIWFRG
RLLVAVSMEV YEGRVEPKPS QTTQRSGLSR LTGKKKKKKE KTRQGQTPAG ILQPASASTS
EDAPEIPSAM EVEVEDLLPL PENALASFED FLLFGVLFEA TMIDPSLAKK PISLEISIGH
AGRQEEQSGQ GSRADEGSES STLEVQPLLE SEDRGAGQEE QELLGTPAQW PEPVDGNGPY
LCLPLRHRKP CLHVWSCWED YTWRLQSSNS VCKVAERLDH GLQEVEKMQR RSGPGACTRL
KQTLEELVAG SRQFCHGAER RTMTRPNALD RCRAKLLTHS LNLMARQGLR LLRSLRLNNM
QRTVVLAKKL LARLRFLAQE PQPPLPDVLV WMFSGQRRVA YARIPAQDIL YSVVEEERGR
DCGKIQSLLL TVPGAAPGEV CAKLELFLWL GLGKQAKACT SELPMDLLPE PSSGLPQSLY
RDDFRYFQLR AHLYQARGVL AADDSGLSDP FARVLISTQC QTTRVLEQTL SPLWDELLVF
DQLIVDGRRE HLREEPPLVV INVFDHNKFG PAVFLGRAFA APRVKLIEDP YQRPELQFFP
LRKGPQAAGE VIATFELIEL DYSGHLEPSV PSDVEPRDLA SLVEPISGHL SLPPSVRPVL
RAFRVEVLFW GLRGLGRVHL FEIEKPQVVL EVAGRRVESE VLPNYRENPN FTELVRHVTV
DLPEQPYLQP PLSILVIERR AFGRTVLVGS HIVPHMLRFI LQGHEDPQEE EETEEETRDL
VPHGPQGEKS LPEAGTSRQL LKAPLKKLTL GLLGQGPELE EDIPDPEEMD WWSKYYASLQ
EFQGQPSSDD EMDEAGDADG THLISGDREA QEQGETDSKV SVPRKKAIAT LKIYNSSLED
EFSHFEDWLS VFPLYRGQGG QDGEGEGASG HFVGKFKGSF LIYPESEAKS FSEPQISRGV
PQNRPIKLLV RVYIVKATNL APADPNGKAD PYVVVSAGKE QRDTKERYIP KQLNPIFGEV
LELSVSLPAQ PELTVAVFDH DLVGSDDLIG ETHIDLENRF YSHHRANCGL ASQYDVNGYN
AWRDAFRPSQ ILAGLCQRCG LPVPEYRAGA VKVGSRVFLT PSEAPPPDDR KPKVTSEASE
EAQALHVLRR WQEMPGLGIQ LVPEHVETRP LYHPRSPGLL QGSLHMWIDI FPSDVPAPPP
VDIKPRQPIS YELRVVIWNT DDVALDDVNP LTGERSSDIY VKSWVKGLEQ DRQETDVHFN
SLTGEGNFNW RFVFRFDYLP TEREVSVRRK PGPFALEEAE FRQPAVLVLQ VWDYDRISAN
DFLGSLELQL PDMVRGARDP EHCSVRLALD GAGPRCNLFR CHRLRGWWPV VKMKDMEDVE
REAREAQAGK KRKRKRRAGR PEDLEFTDTG GNVYILTGKV EAEFELLTVE EAEKRPVGKG
RKEPEPLEKP NRPKTSFNWF VNPLKTFIFF IWRRYWRILV LLLLALITIF LLLVFYTIPG
QISEVIFSPV HK