KTN1_VULVU
ID KTN1_VULVU Reviewed; 1330 AA.
AC O97961;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 77.
DE RecName: Full=Kinectin;
GN Name=KTN1;
OS Vulpes vulpes (Red fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX NCBI_TaxID=9627;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Testis;
RX PubMed=11933159; DOI=10.1002/mrd.10066;
RA Xu J., Bird P.H., Bradley M.P., Janssens P.A., Hardy C.M.;
RT "Molecular cloning and characterization of fox testis kinectin.";
RL Mol. Reprod. Dev. 62:37-46(2002).
CC -!- FUNCTION: Receptor for kinesin thus involved in kinesin-driven vesicle
CC motility. {ECO:0000250}.
CC -!- SUBUNIT: Parallel homodimers formed between the membrane-bound and the
CC cytosolic form, and also between 2 cytosolic forms. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type
CC II membrane protein. Note=Vesicle membrane protein anchored to the
CC endoplasmic reticulum. In testis, localized at sperm surface.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=O97961-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O97961-2; Sequence=VSP_007983;
CC Name=3;
CC IsoId=O97961-3; Sequence=VSP_007984;
CC -!- TISSUE SPECIFICITY: Expressed in male brain, heart, kidney, liver,
CC lung, spleen and testis.
CC -!- SIMILARITY: Belongs to the kinectin family. {ECO:0000305}.
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DR EMBL; AF095786; AAC64407.1; -; mRNA.
DR AlphaFoldDB; O97961; -.
DR SMR; O97961; -.
DR STRING; 9627.ENSVVUP00000041588; -.
DR Proteomes; UP000286640; Unplaced.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IEA:InterPro.
DR GO; GO:0019894; F:kinesin binding; IEA:InterPro.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; IEA:InterPro.
DR InterPro; IPR024854; Kinectin.
DR InterPro; IPR007794; Rib_rcpt_KP.
DR PANTHER; PTHR18864; PTHR18864; 1.
DR Pfam; PF05104; Rib_recp_KP_reg; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Coiled coil; Endoplasmic reticulum; Glycoprotein;
KW Membrane; Phosphoprotein; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..1330
FT /note="Kinectin"
FT /id="PRO_0000084338"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..29
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..1330
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 49..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 108..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 332..1329
FT /evidence="ECO:0000255"
FT COMPBIAS 63..81
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..139
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..186
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..218
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86UP2"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86UP2"
FT MOD_RES 153
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q86UP2"
FT MOD_RES 156
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86UP2"
FT MOD_RES 1085
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86UP2"
FT MOD_RES 1286
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86UP2"
FT CARBOHYD 172
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 435
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 772
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 904
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1055
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1236
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1302
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 834..856
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11933159"
FT /id="VSP_007983"
FT VAR_SEQ 1031..1060
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11933159"
FT /id="VSP_007984"
SQ SEQUENCE 1330 AA; 153478 MW; CDCDD415B274F42B CRC64;
MEFYESTYFI VLIPSVVITV IFLFFWLFMK ETLYDEVLAK QKREQKLIPT KTDKKKAEKK
KNKKKEIQNG NLHESDSESV PRDFKLSDAL AVEDEQVVPI PLNVVETSSS VRERKKKEKK
HKPVLEEQVT KESDVSKIPG KKVEPVPVTK QPTPPSEAAA SKKKPGQKKS KNGSDDQDKK
VETLMAPSKK QESLPLQQET KQESGSGKKK VSSKKQKAEN VLVDEPLIHA TTYIPLMDNA
DSNPVLDKRE VIDLIKPDQV EGIQKTGAKK LKTETDKENA EVKFKDFLLS LKTMMFSEDE
ALCVVDLLKE KSGVIQDALK RSSKGELTAL VHQLQEKDKL LAAVKEDAAV MKDRCKQLTQ
EMMSEKERSN VVIARMKDRI GTLEKEHNVF QNKMHVSYQE TQQMQMKFQQ VREQMEAEIA
HLKQENGILR DAVSNTTNQL ESKQSAELNK LRQDYARLVN ELTEKTGKLQ QEEVQKKNAE
QAVTQLKVQL QEAERRWEEV QSYIRKRTAE HEAAQQDLQS KFVAKENEVQ SLHSKLTDTL
VSKQQLEQRL MQLMESEQKR VTKEESLQMQ VQDILEQNEA LKALIQQFHS QIAAQTSASV
LAEELHKVIA EKDKQIKQTE DSLANEHDHL TSKEEELKDI QNMNFLLKAE VQKLQALANE
QAAAAHELEK MQKSIHVKDD QIRLLEEQLQ CEISNKMEEF KILNDQNKAL QLEVQKLQIL
VSEQPNKDVV EQMEKCIQEK DEKLKTVEEL LETGLIQVAT KEEELNAIRT ENSSLTKEVQ
DLKAKQNDQV SFASLVEELK KVIHEKDGKI KSVEELLEAE VLKVANKEKT IQDLKQEIEA
LKEEIGNIQL EKAQQLSITS QIQELQNLLK GKEEQMNTMK TVLEEKEKDL ASRGKWLQDL
QEENESLKTH IQEVAQHNLK EACSASRLEE LETVLKEKEN EMKRIETILK ERENDLSSKI
KLLQEVQDEN KLFKSEIEQL KQCNYQQASS FPPHEELLKV ISEREKEITG LQNELDSLKE
AVEHQRKKNN DLREKNWEAM EALASTEKML QDKVNKTSKV ERQQYVEAIE LEAKEVLKKL
FPKVSVPPNL NYGEWLRGFE KKPKECVAET SGSEEVKVLE HKLKEADEMH TLLQLECEKY
KSVLAETEGI LQKLQRSVEQ EENKWKVKVD ESQKTIKQMQ LSFTSSEQEL ERLRRENKDI
ENLRREREHL EMELEKAEIE RSTYVTEVRE LKTQLNETLT KLRTEQSERQ KVAGDLHKAQ
QSLDLIQSKI VKAAGDTTVI ENSDVSPEAE SSEKETMSVS LNQTVTQLQQ LLQAVNQQLT
KEKEHYQVLE
