ID H2ZYG2_LATCH Unreviewed; 1319 AA.
AC H2ZYG2;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Sperm associated antigen 9 {ECO:0000313|Ensembl:ENSLACP00000002433.1};
GN Name=SPAG9 {ECO:0000313|Ensembl:ENSLACP00000002433.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000002433.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000002433.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the JIP scaffold family.
CC {ECO:0000256|ARBA:ARBA00009866}.
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DR EMBL; AFYH01118706; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01118707; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01118708; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01118709; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01118710; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01118711; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01118712; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01118713; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSLACT00000002453.1; ENSLACP00000002433.1; ENSLACG00000002172.2.
DR GeneTree; ENSGT00940000153496; -.
DR HOGENOM; CLU_003841_0_0_1; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR Bgee; ENSLACG00000002172; Expressed in muscle tissue and 6 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005078; F:MAP-kinase scaffold activity; IEA:InterPro.
DR Gene3D; 1.20.58.1770; -; 1.
DR Gene3D; 1.20.5.1000; arf6 gtpase in complex with a specific effector, jip4; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR039911; JIP3/JIP4.
DR InterPro; IPR032486; JIP_LZII.
DR InterPro; IPR019143; JNK/Rab-associated_protein-1_N.
DR InterPro; IPR034743; RH1.
DR InterPro; IPR034744; RH2.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR13886:SF2; C-JUN-AMINO-TERMINAL KINASE-INTERACTING PROTEIN 4; 1.
DR PANTHER; PTHR13886; JNK/SAPK-ASSOCIATED PROTEIN; 1.
DR Pfam; PF16471; JIP_LZII; 1.
DR Pfam; PF09744; Jnk-SapK_ap_N; 1.
DR Pfam; PF19056; WD40_2; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS51776; RH1; 1.
DR PROSITE; PS51777; RH2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000008672}.
FT DOMAIN 6..94
FT /note="RH1"
FT /evidence="ECO:0000259|PROSITE:PS51776"
FT DOMAIN 487..557
FT /note="RH2"
FT /evidence="ECO:0000259|PROSITE:PS51777"
FT REGION 214..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 567..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 793..825
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 853..874
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 60..161
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 432..515
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 714..741
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 224..246
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..273
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 805..825
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1319 AA; 146718 MW; 99FBF495B857E74F CRC64;
MELEDGVVYQ DDPGTAAMMS ERVSGLASSI YREFERLIGK YDEDVVKDLM PLVVAVLENL
DTVFAENQEH EVELELLKED NEQLITQYER EKALRKHAEE KFIEFEDSQE QEKKDLQGRV
EVLESQTRQL ELKAKNYADQ ISRLEEREAE LKKEYGSLHQ RHTEMIHNYM EHLERTKLQQ
LLGGDQLESM THGRIRKERP ISLGIFPLPG GDALLTPDTQ REGADTPGTE HWRFHDLSHP
RSNTSLKDEL SDVSQGGSKS ATPLSTATSD IPMPSIDTPL KEEAEGAVIN ANTTNIKQDI
SKNIEVQVVQ ETRTVSTGST ENEEKSDVQA IIESTPELDM DKDLSGCGIT STPTKGIENK
AFDRNTESLF EELSSAGSGL IGDVDEGADL LGMGREVENL ILENTQLLET KNALNIVKND
LIMKVDELTC ERQVLVGELE AVKQAKQKLE EKNRDLEEEL KKVRAEVEEA KQKAKEEDDS
DVPTAQRKRF TRVEMARVLM ERNQYKERLM ELQEAVRWSE MIRASRESPA MQEKKRSSIW
QFFSRLFGPS SNTTKKLEHP VNVKYNAPTS HITPSVKKRS STLSQLPSDK SKAFDFLEEN
ESSLASRREQ KREQYRQVKV HVQKEDGRVQ ACGWSLPQKY KQVTNGGQGE NKMKNLPVPV
YLRPLDEKDA SMKLWCAAGV NLSGGKTRDG GSIIGASVFY NDVSGSEIEG SKQQRGSQSS
LDRLEQELKE QEKELKQQDE LSSVVWICTS TQSASKVIII DANQPGNILD NFFVCNSHVL
CIASVPGARE TDYPAGEEIP RDADFSQADN SSLGGSAASN SSAGNESMLG GITVVGCNIE
GTAAPQNVQT VANVSPMPEK QTDTDAESGG VENIPTAEEA TEATEANAGS GEELIDVSQT
GIYTEHVFID PLGVQNTSDT LPTYQQSSET DVVSTLPDEQ DLMREEAQKM SSVLPTMWLG
AQNGCLYVHS SVAQWKKCLH SIKLKDSILS IVHVKGRVLV ALADGTLAIF HRGIDGQWDL
TNYHLLDLGR PLHSIRCMTV VHDKVWCGYR NKIYVVQPKA MKIEKSFDAH PRRESQVRQL
AWVGDGVWVS IRLDSTLRLY HVHTYQHLQD VDIEPYVSKM LGTGKLGFSF VRITALMVSC
NRLWVGTGNG VIISIPLTET VILHQGRLLG LRANKVSGTT GSRPGNVIRV YGDENSDKVT
PGTFIPYCSM AHAQLCFHGH RDAVKFFVAV PGQVICPQSS TNTDPFCEKA RPSASDITNQ
QLLKSMLVVS GGEGYIDFRM GDEGGESEEL LGEALQLQSS LAKAERSHLI VWQVMCDNE
//
