ID A0A2I2U1K4_FELCA Unreviewed; 2774 AA.
AC A0A2I2U1K4;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 2.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Teneurin transmembrane protein 2 {ECO:0000313|Ensembl:ENSFCAP00000026331.2};
GN Name=TENM2 {ECO:0000313|Ensembl:ENSFCAP00000026331.2,
GN ECO:0000313|VGNC:VGNC:66070};
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000026331.2, ECO:0000313|Proteomes:UP000011712};
RN [1] {ECO:0000313|Ensembl:ENSFCAP00000026331.2, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000026331.2,
RC ECO:0000313|Proteomes:UP000011712};
RX PubMed=17975172; DOI=10.1101/gr.6380007;
RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA Tesler G., O'Brien S.J.;
RT "Initial sequence and comparative analysis of the cat genome.";
RL Genome Res. 17:1675-1689(2007).
RN [2] {ECO:0000313|Ensembl:ENSFCAP00000026331.2, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000026331.2,
RC ECO:0000313|Proteomes:UP000011712};
RA Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT "Sequence assembly of the Felis catus genome version 6.2.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSFCAP00000026331.2}
RP IDENTIFICATION.
RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000026331.2};
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004162};
CC Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004162}. Membrane
CC {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004167}.
CC -!- SIMILARITY: Belongs to the tenascin family. Teneurin subfamily.
CC {ECO:0000256|ARBA:ARBA00009385}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; AANG04001174; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_019694739.1; XM_019839180.1.
DR STRING; 9685.ENSFCAP00000026331; -.
DR Ensembl; ENSFCAT00000040468.3; ENSFCAP00000026331.2; ENSFCAG00000007084.6.
DR VGNC; VGNC:66070; TENM2.
DR GeneTree; ENSGT01030000234566; -.
DR InParanoid; A0A2I2U1K4; -.
DR OMA; MCEPSPH; -.
DR Proteomes; UP000011712; Chromosome A1.
DR Bgee; ENSFCAG00000007084; Expressed in zone of skin and 9 other cell types or tissues.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0050839; F:cell adhesion molecule binding; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; IBA:GO_Central.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IBA:GO_Central.
DR GO; GO:0048666; P:neuron development; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd00054; EGF_CA; 3.
DR Gene3D; 2.10.25.10; Laminin; 6.
DR Gene3D; 2.180.10.10; RHS repeat-associated core; 1.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 2.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR008969; CarboxyPept-like_regulatory.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR011044; Quino_amine_DH_bsu.
DR InterPro; IPR022385; Rhs_assc_core.
DR InterPro; IPR009471; Ten_N.
DR InterPro; IPR028916; Tox-GHH_dom.
DR InterPro; IPR006530; YD.
DR NCBIfam; TIGR03696; Rhs_assc_core; 1.
DR NCBIfam; TIGR01643; YD_repeat_2x; 1.
DR PANTHER; PTHR11219; TENEURIN AND N-ACETYLGLUCOSAMINE-1-PHOSPHODIESTER ALPHA-N-ACETYLGLUCOSAMINIDASE; 1.
DR PANTHER; PTHR11219:SF8; TENEURIN-2; 1.
DR Pfam; PF06484; Ten_N; 1.
DR Pfam; PF15636; Tox-GHH; 1.
DR SMART; SM00181; EGF; 8.
DR SMART; SM00179; EGF_CA; 2.
DR SUPFAM; SSF49464; Carboxypeptidase regulatory domain-like; 1.
DR SUPFAM; SSF101898; NHL repeat; 1.
DR SUPFAM; SSF50969; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR PROSITE; PS00022; EGF_1; 5.
DR PROSITE; PS01186; EGF_2; 4.
DR PROSITE; PS50026; EGF_3; 3.
DR PROSITE; PS51361; TENEURIN_N; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000011712};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 375..400
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..375
FT /note="Teneurin N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51361"
FT DOMAIN 668..700
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 702..735
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 806..841
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 21..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 111..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 690..699
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 725..734
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 810..820
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 831..840
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 2774 AA; 307435 MW; A58927DE713E0E10 CRC64;
MDVKDRRHRS LTRGRCGKEC RYTSSSLDSE DCRVPTQKSY SSSETLKAYD HDSRMHYGNR
VTDLVHRESD EFPRQGTNFT LAELGMCEPS PHRSGYCSDM GILHQGYSLS TGSDADSDTE
GGMSPEHAIR LWGRGIKSRR SSGLSSRENS ALTLTDSDNE NKSDDENGRP IPPTSSSSLL
PSAQLPSSHN PPPVSCQMPL LDSNTSHQIM DTNPDEEFSP NSYLLRACSG PQQASSSGPP
NHHSQSTLRP PLPPPHNHTL SHHHSSANSL NRNSLTNRRS QIHAPAPAPN DLATTPESVQ
LQDSWVLNSN VPLETRHFLF KTSSGSTPLF SSSSPGYPLT SGTVYTPPPR LLPRNTFSRK
AFKLKKPSKY CSWKCAALSA IAAALLLAIL LAYFIAMHLL GLNWQLQPAD GHTFNNGIRT
GLPGSDDVAT MPSGGKVPWS LKNSSIDSGE AEVGRRVTQE VPPGVFWRSQ IHISQPQFLK
FNISLGKDAL FGVYIRRGLP PSHAQYDFME RLDGKEKWSV VESPRERRSI QTLVQNEAVF
VQYLDVGLWH LAFYNDGKDK EMVSFNTVVL DSVQDCPRNC HGNGECVSGL CHCFPGFLGA
DCAKAACPVL CSGNGQYSKG TCQCYSGWKG AECDVPMNQC IDPSCGGHGS CIDGNCVCSA
GHKGEHCEEV DCLDPTCSSH GVCVNGECLC SPGWGGLNCE LARVQCPDQC SGHGTYVPDT
GLCSCDPNWM GPDCSVEVCS VDCGTHGVCI GGACRCEEGW TGAACDQRVC HPRCIEHGTC
KDGKCECREG WNGEHCTIGR QTAGTETDGC PDLCNGNGRC TLGQNSWQCV CQTGWRGPGC
NVAMETSCAD NKDNEGDGLV DCLDPDCCLQ SACQNSLLCR GSRDPLDIIQ QGQTDSPAVK
SFYDRIKLLA GKDSTHIIPG DNPFNSSLVS LIRGQVVTTD GTPLVGVNVS FVKYPKYGYT
ITRQDGTFDL IANGGASLTL HFERAPFMSQ ERTVWLPWNS FYAMDTLVMK TEENSIPSCD
LSGFVRPDPI IISSPLSTFF SAAPGQNPIV PETQVLHEEI ELPGSTVKLR YLSSRTAGYK
SLLKITMTQS TVPLNLIKVH LMVAVEGHLF QKSFQASPNL AYTFIWDKTD AYGQRVYGLS
DAVVSVGFEY ETCPSLILWE KRTALLQGFE LDPSNLGGWS LDKHHILNVK SGILHKGTGE
NQFLTQQPAI ITSIMGNGRR RSISCPSCNG LAEGNKLLAP VALAVGIDGS LFVGDFNYIR
RIFPSRNVTS ILELRNKEFK HSNNPAHKYY LAVDPVSGSL YVSDTNSRRI YRVKSLSGAK
DLAGNSEVVA GTGEQCLPFD EARCGDGGKA VDATLMSPRG IAVDKNGLMY FVDATMIRKV
DQNGIISTLL GSNDLTAVRP LSCDSSMDVA QVRLEWPTDL AVNPMDNSLY VLENNVILRI
TENHQVSIIA GRPMHCQVPG IDYSLSKLAI HSALESASAI AISHTGVLYI TETDEKKINR
LRQVTTNGEI CLLAGAASDC DCKNDVNCNC YSGDDAYATD AILNSPSSLA VAPDGTIYIA
DLGNIRIRAV SKNKPVLNAF NQYEAASPGE QELYVFNADG IHQYTVSLVT GEYLYNFTYS
ADNDVTELID NNGNSLKIRR DSSGMPRHLL MPDNQIITLT VGTNGGLKVV STQNLELGLM
TYDGNTGLLA TKSDETGWTT FYDYDHEGRL TNVTRPTGVV TSLHREMEKS ITIDIENSNR
DDDVTVITNL SSVEASYTVV QDQVRNSYQL CNNGTLRVMY ANGMGVSFHS EPHVLAGTIT
PTIGRCNISL PMENGLNSIE WRLRKEQIKG KVTIFGRKLR VHGRNLLSID YDRNIRTEKI
YDDHRKFTLR IIYDQVGRPF LWLPSSGLAA VNVSYFFNGR LAGLQRGAMS ERTDIDKQGR
IVSRMFADGK VWSYSYLDKS MVLLLQSQRQ YIFEYDSSDR LHAVTMPSVA RHSMSTHTSI
GYIRNIYNPP ESNASVIFDY SDDGRILKTS FLGTGRQVFY KYGKLSKLSE IVYDSTAVTF
GYDETTGVLK MVSLQSGGFS CTIRYRKIGP LVDKQIYRFS EEGMVNARFD YTYHDNSFRI
ASIKPVISET PLPVDLYRYD EISGKVEHFG KFGVIYYDIN QIITTAVMTL SKHFDTHGRI
KEVQYEMFRS LMYWMTVQYD SMGRVIKREL KLGPYANTTK YTYDYDGDGQ LQSVAVNDRP
TWRYSYDLNG NLHLLNPGNS VRLMPLRYDL RDRITRLGDV QYKIDDDGYL CQRGADIFEY
NSKGLLTRAY NKASGWSVQY RYDGVGRRAS YKTNLGHHLQ YFYSDLHNPT RITHVYNHSN
SEITSLYYDL QGHLFAMESS SGEEYYVASD NTGTPLAVFS INGLMIKQLQ YTAYGEIYYD
SNPDFQMVIG FHGGLYDPLT KLVHFTQRDY DVLAGRWTSP DYTMWKNVGK EPAPFNLYMF
KSNNPLSNEL DLKNYVTDVK SWLVMFGFQL SNIIPGFPRA KMYFVPPPYE LSESQASENG
QLITGVQQTT ERHNQAFMAL EGQVISKKLH ANIREKAGHW FATTTPIIGK GVMFAIKEGQ
VTTGVSSVAS EDSRKVASVL NNAYYLDKMH YSIEGKDTHY FVKIGSADGD LVTLGTTIGR
KVLESGVNVT VSQPTLLVNG RTRRFTNIEF QYSTLLLSIR YGLTPDTLDE EKARVLDQAR
QRALGTAWAK EQQKARDGRE GSRLWTEGEK QQLLSTGRVQ GYEGYYVLPV EQYPELADSS
SNIQFLRQNE MGKR
//
